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Information on EC 1.1.1.34 - hydroxymethylglutaryl-CoA reductase (NADPH)
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EC Tree
1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH)IUBMB Comments
The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
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Word Map
- 1.1.1.34
- cholesterol
- statin
- lipoprotein
- simvastatin
- sterol
- cardiovascular
- triglyceride
-
low-density
- hypercholesterolemia
- lovastatin
- pravastatin
- coronary
-
lipid-lowering
- bile
- endothelial
- artery
- atorvastatin
- atherosclerosis
-
isoprenoids
- hdl
-
cholesterol-lowering
- hyperlipidemia
-
ldl-cholesterol
-
placebo
- squalene
-
apolipoproteins
- myopathy
-
hypocholesterolemic
-
farnesylation
-
geranylgeranylation
-
hypolipidemic
- rosuvastatin
- dyslipidemias
-
high-density
-
fibrates
- cyp7a1
- cholestyramine
- rhabdomyolysis
-
7alpha-hydroxylase
- drug development
- medicine
- nutrition
-
acyl-coa:cholesterol
- molecular biology
- 25-hydroxycholesterol
- lanosterol
- gemfibrozil
- pcsk9
- ezetimibe
- biotechnology
- dolichols
-
isoprenylation
- srebp-2
-
statin-induced
-
lipoprotein-cholesterol
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
2
=
+
2
+
2
Synonyms
hmg-coa reductase, hmgcr, 3-hydroxy-3-methylglutaryl coenzyme a reductase, hmgr, hmg coa reductase, 3-hydroxy-3-methylglutaryl-coa reductase, 3-hydroxy-3-methylglutaryl-coenzyme a reductase, hmgcoa reductase, 3-hydroxy-3-methylglutaryl coa reductase, hmg-coar, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy-3-methylglutaryl CoA reductase
3-hydroxy-3-methylglutaryl coenzyme A reductase
3-hydroxy-3-methylglutaryl-CoA reductase
3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)
-
-
-
-
3-hydroxy-3-methylglutaryl-coenzyme A reductase
acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme A reductase
-
-
beta-hydroxy-beta-methylglutaryl coenzyme A reductase
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-
-
-
beta-hydroxy-beta-methylglutaryl-Co A reductase
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-
-
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HMG-CoA reductase
HMG-CoAR
HMG1
HMG2
HMG2.2
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-
-
-
HMG3.3
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-
-
-
HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating CoA)
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-
-
-
HMGCR
HMGR
HMGR1
HMGR1S
HMGR2
HMGR3
hydroxymethylglutaryl CoA reductase (NADPH)
-
-
-
-
hydroxymethylglutaryl-coenzyme A reductase (reduced nicotinamide adenine dinucleotide phosphate)
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-
-
-
mevalonate:NADP+ oxidoreductase (acetylating CoA)
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-
-
-
NADPH-hydroxymethylglutaryl-CoA reductase
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-
-
-
S-3-hydroxy-3-methylglutaryl-CoA reductase
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-
-
-
3-hydroxy-3-methylglutaryl-CoA reductase
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-
-
-
HMG-CoA reductase
-
-
-
-
HMGR
-
-
-
-
HMGR1
-
-
-
-
HMGR2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Glu559 and His866 are involved in catalysis
-
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
via mevaldehyde as an intermediate product
-
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
via mevaldehyde as an intermediate product, enzyme contains a catalytic His381, Lys267 is also involved in catalysis, active site structure
-
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
reaction mechanism, modelling of three different systems, detailed overview. Formation of a mevaldyl-CoA intermediate protonated by a conserved active site lysine, Lys691. The conserved active site glutamate and aspartate residues, Glu559 and Asp767, along with the ribose moiety of NADPH, form a hydrogen bond network crucial to the increase of the stabilizing effect of Lys691 over the transition state. A charged His752 forms an oxyanion hole with Lys691 to stabilize the negative charge developed in the thioester oxygen
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(R)-mevalonate:NADP+ oxidoreductase (CoA-acylating)
The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
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CAS REGISTRY NUMBER
COMMENTARY
9028-35-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-mevalonate + CoA + NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldehyde + CoA + NADP+
-
first step reaction
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
DL-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
-
second step reaction
-
-
?
(R)-mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
second step of the reaction
-
-
?
(R)-mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
second step of the reaction
-
-
?
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
?
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ochromonas malhamensis
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-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R,S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(R,S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + 2 NADP+ + CoA
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + 2 NADP+ + CoA
-
HMGR is a key enzyme in the mevalonate pathway of isoprenoid biosynthesis, the sole route in haloarchaea for lipid and carotenoid production
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
enzyme is essential for sterol biosynthesis
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
involved in isopentenyl diphosphate biosynthesis, mevalonate pathway overview
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
overall reaction
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
overall reaction
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
overall reaction
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
the enzyme is implicated in latex metabolism
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
Ochromonas malhamensis
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
overall reaction
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
the reduction of 3-hydroxy-3-methylglutaryl-CoA is preferred over oxidation of mevalonate
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
-
first step reaction
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
-
first step reaction
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
rate-limiting step of cholesterol biosynthesis
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?, r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
first step reaction
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
substrate is (S)-isomer of HMG-CoA
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
substrate is (S)-isomer of HMG-CoA
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
ir
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
up- and down-regulation of HMGR activity in response to changes in the flux of the mevalonate pathway occur via post-translational control
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
Neophaeotheca triangularis MZKI B741
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
key enzyme of the mevalonic acid pathway catalysing the first committed step with NADPH as cofactor, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
HMGR is the key regulatory enzyme of the mevalonate pathway and also the iridoid biosynthesis, it is highly regulated itself, HMGR may represent a regulator in maintenance of homeostasis between de novo produced and sequestered intermediates of iridoid metabolism, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
the enzyme utilizes two molecules of NADPH to mediate the four-electron reduction of HMG-CoA to the carboxylic acid mevalonate, homology modeling of the catalytic domain
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
-
second step reaction
-
-
r
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
-
third step reaction
-
-
r
additional information
?
-
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
?
additional information
?
-
-
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
?
additional information
?
-
-
phytosterol biosynthetic pathway, overview
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
?
additional information
?
-
-
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
HMG-CoA reductase is regulated by salinity at the level of transcription
-
-
?
additional information
?
-
-
the expression of HMGR is regulated in response to non-optimal salinity in the halophilic archaeon
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
enzyme plays a central role in sterol biosynthesis, investigation of the physiological regulation, 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
the reaction is a highly regulated process within the cholesterol biosynthetic pathway
-
-
?
additional information
?
-
-
method development for rapid and versatile reverse phase -HPLC monitoring for assaying HMGR activity capable of monitoring the levels of both substrates HMG-CoA and NADPH, and products CoA, mevalonate, and NADP+, method evaluation, overview
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
ubiquitination and proteasomal degradation of microsomal, but not mitochondrial, HMGR isozymes depends on environmental salinity, overview
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
rate-limiting enzyme in the biosynthesis of cholesterol in mammals
-
-
?
additional information
?
-
-
small heterodimer partner nuclear receptor directly regulates cholesterol biosynthesis through inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase
-
-
?
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
?
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
Ochromonas malhamensis
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
HMGR activity is not only diminished in iridoid producers but most likely prevalent within the Chrysomelina subtribe and also within the insecta
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
enzyme undergoes endoplasmic reticulum-associated degradation which is physiologically regulated by sterol pathway signals, determination of structural features leading to modification and degradation by the quality control system of the endoplasmic reticulum, overview
-
-
?
additional information
?
-
enzyme in the pathway for production of prenyl alcohols. Almost all Saccharomyces cerevisiae strains tend to produce mainly squalene and low amount of prenyl alcohols. Among these ATCC strains, relatively large amounts of prenyl alcohols in the cultures of two recombinants (ATCC201741 and ATCC 200027). Amounts are quite low compared to the case of ATCC 200589 recombinant. These differences possibly depend on the difference in the squalene synthase activity. If the enzyme activity is weaker in ATCC 200589, the activation of the pathways will result in the accumulation of (E,E)-farnesyl diphosphate, the substrate of the enzyme, and following production of (E,E)-farnesol through hydrolysis of (E,E)-farnesyl diphosphate. Recombinant AURGG101 derived from ATCC 200589 produces large amounts of prenyl alcohols. In particular, (E,E)-farnesol in AURGG101 reaches 35.6 mg/l, which is approximately 4fold higher than that in ATCC 200589. HMG1 expression in strain ATCC 200589 increases the production of squalene, (E)-nerolidol, (E,E)-farnesol, and (E,E,E)-geranylgeraniol, whereas that in ATCC 76625 causes high squalene production, low production of (E,E)-farnesol and (E,E,E)-geranylgeraniol, and no (E)-nerolidol production
-
-
?
additional information
?
-
-
enzyme in the pathway for production of prenyl alcohols. Almost all Saccharomyces cerevisiae strains tend to produce mainly squalene and low amount of prenyl alcohols. Among these ATCC strains, relatively large amounts of prenyl alcohols in the cultures of two recombinants (ATCC201741 and ATCC 200027). Amounts are quite low compared to the case of ATCC 200589 recombinant. These differences possibly depend on the difference in the squalene synthase activity. If the enzyme activity is weaker in ATCC 200589, the activation of the pathways will result in the accumulation of (E,E)-farnesyl diphosphate, the substrate of the enzyme, and following production of (E,E)-farnesol through hydrolysis of (E,E)-farnesyl diphosphate. Recombinant AURGG101 derived from ATCC 200589 produces large amounts of prenyl alcohols. In particular, (E,E)-farnesol in AURGG101 reaches 35.6 mg/l, which is approximately 4fold higher than that in ATCC 200589. HMG1 expression in strain ATCC 200589 increases the production of squalene, (E)-nerolidol, (E,E)-farnesol, and (E,E,E)-geranylgeraniol, whereas that in ATCC 76625 causes high squalene production, low production of (E,E)-farnesol and (E,E,E)-geranylgeraniol, and no (E)-nerolidol production
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + 2 NADP+ + CoA
-
HMGR is a key enzyme in the mevalonate pathway of isoprenoid biosynthesis, the sole route in haloarchaea for lipid and carotenoid production
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
-
first step reaction
-
-
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
rate-limiting step of cholesterol biosynthesis
-
-
r
D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
-
second step reaction
-
-
?
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
?
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ochromonas malhamensis
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
enzyme is essential for sterol biosynthesis
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
involved in isopentenyl diphosphate biosynthesis, mevalonate pathway overview
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
the enzyme is implicated in latex metabolism
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
Ochromonas malhamensis
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
ir
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
up- and down-regulation of HMGR activity in response to changes in the flux of the mevalonate pathway occur via post-translational control
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
Neophaeotheca triangularis MZKI B741
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
key enzyme of the mevalonic acid pathway catalysing the first committed step with NADPH as cofactor, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
HMGR is the key regulatory enzyme of the mevalonate pathway and also the iridoid biosynthesis, it is highly regulated itself, HMGR may represent a regulator in maintenance of homeostasis between de novo produced and sequestered intermediates of iridoid metabolism, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
additional information
?
-
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
?
additional information
?
-
-
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
?
additional information
?
-
-
phytosterol biosynthetic pathway, overview
-
-
?
additional information
?
-
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
?
additional information
?
-
-
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
?
additional information
?
-
-
HMG-CoA reductase is regulated by salinity at the level of transcription
-
-
?
additional information
?
-
-
the expression of HMGR is regulated in response to non-optimal salinity in the halophilic archaeon
-
-
?
additional information
?
-
-
enzyme plays a central role in sterol biosynthesis, investigation of the physiological regulation, 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols
-
-
?
additional information
?
-
-
the reaction is a highly regulated process within the cholesterol biosynthetic pathway
-
-
?
additional information
?
-
-
ubiquitination and proteasomal degradation of microsomal, but not mitochondrial, HMGR isozymes depends on environmental salinity, overview
-
-
?
additional information
?
-
-
small heterodimer partner nuclear receptor directly regulates cholesterol biosynthesis through inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase
-
-
?
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
?
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
?
additional information
?
-
-
HMGR activity is not only diminished in iridoid producers but most likely prevalent within the Chrysomelina subtribe and also within the insecta
-
-
?
additional information
?
-
-
enzyme undergoes endoplasmic reticulum-associated degradation which is physiologically regulated by sterol pathway signals, determination of structural features leading to modification and degradation by the quality control system of the endoplasmic reticulum, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
NaCl
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
NaCl
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R,5R)-7-(1-ethyl-3-(4-fluorophenyl)-4-methyl-5-[(5-methyl-pyrazin-2-ylmethyl)-carbamoyl]-1H-pyrrol-2-yl)-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-4-methyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxybenzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxycarbonyl-benzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluoro-phenyl)-1-isopropyl-5-phenylcarbamoyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluorophenyl)-1-isopropyl-4-phenyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluorophenyl)-5-[(3-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[3-(4-fluorophenyl)-5-[[4-(methoxymethyl)benzyl]carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[5-(4-carboxy-benzylcarbamoyl)-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid disodium salt
-
-
(3R,5R)-7-[5-benzylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid
-
-
(3R,5R)-7-[5-carbamoyl-1-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[5-carbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid sodium salt
-
-
(3R,5R)-7-[5-cyano-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
(3R,5R)-7-[5-[(3-carbamoylbenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[5-[(4-cyanobenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[5-[[4-(dimethylcarbamoyl)benzyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(5S)-5-hydroxy-4-{2-[(1S,2R,4aR)-1,2,4a,5-tetramethyl-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-yl]ethyl}furan-2(5H)-one
-
22.65% inhibition of HMG-CoA reductase at 0.001 mM concentration and maximum inhibition of 78.03% at 0.1 mM, the HMG-CoA reductase inhibitor, a clerodane diterpene from ethanolic extract of Polyalthia longifolia var. pendula, is a potential lipid lowering agent, molecular docking analysis, overview
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
-
competitive inhibitor, shows slight inhibitory activity
4-[[([5-[(3R,5R)-6-carboxy-3,5-dihydroxyhexyl]-4-(4-fluorophenyl)-1-(1-methylethyl)-3-phenyl-1H-pyrrol-2-yl]carbonyl)amino]methyl]benzoic acid
-
-
7-[3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3,4-bis(4-fluorophenyl)-5-[(3-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3,4-bis(4-fluorophenyl)-5-[(3-methoxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(propylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(4-sulfamoylphenyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(pyridin-2-ylmethyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(4-methyl-1,3-thiazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-imidazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-pyrazol-3-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-5-(methylcarbamoyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-5-[(4-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-5-[(4-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(benzylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(cyclopropylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(dimethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(ethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-carbamoyl-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-ethylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
7-[5-[(4-carbamoylphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[(4-carboxyphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[[(1,5-dimethyl-1H-pyrazol-3-yl)methyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[[3-(dimethylcarbamoyl)phenyl]carbamoyl]-3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[[4-(dimethylcarbamoyl)phenyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
8-hydroxygeraniol
-
competitive inhibition mechanism, binds at the catalytic site, docking experiments, overview
adenosine-2'-monophospho-5'-diphosphoribose
-
competitive inhibitor for NADPH binding site
brutieridin
i.e. hesperetin 7-(2''-alpha-rhamnosyl-6''-(3''''-hydroxy-3''''-methylglutaryl)-beta-D-glucoside), a flavonoid conjugate from bergamot fruit extract, structural analogue of statins, computational study, overview
ceramide
-
treatment with exogenous ceramides, or increasing the endogenous ceramide levels inhibits HMGCR by 6080%
CoA disulfide
-
no inactivation in presence of NADPH 1 mM, or HMG-CoA 0.5 mM
daidzein
-
isoflavone, isolated and purified from korean soybean paste, structural analysis
EDTA
-
inhibits the subsequent reactions of the mevalonate pathway in Hevea latex
eicosapentaenoic acid
-
inhibits translation of the enzyme about 50% at 0.15 mM, downregulation, slightly increases downregulation of protein synthesis by cycloheximide
genistein
-
isoflavone, isolated and purified from korean soybean paste, structural analysis
GFPDGG
-
designed on the basis of the rigid peptide backbone, increases the inhibitory potency more than 300 times compared to the first isolated LPYP from soybean, overview
glycitein
-
isoflavone, isolated and purified from korean soybean paste, structural analysis
melitidin
i.e. naringenin 7-(2''-alpha-rhamnosyl-6''-(3''''-hydroxy-3''''-methylglutaryl)-beta-D-glucoside), a flavonoid conjugate from bergamot fruit extract, structural analogue of statins, computational study, overview
methyl (2-methoxy-5-nitro-4-propylphenoxy)acetate
-
96.8% inhibition at 0.1 mM
myriocin
-
concomitant reduction of both HMGR activity and the sterol content by depletion of the sphingolipid pathway. At 0.01 mM myriocin decrease to ca. 55% of the HMGR activity in control plants. Myriocin-induced down-regulation of HMGR activity is exerted at the post-translational level, like the regulatory response of HMGR to enhancement or depletion of the flux through the sterol pathway
resveratrol
inhibits the cell growth as well as the activity of recombinant enzyme. Resveratrol shows antitrypanosomal activity with an IC50 value of 0.00013 mM and moderate antipromastigote activity against Leishmania major with IC50 value: 0.153 mM
SFGYVAE peptide
-
most active inhibitory peptide; shows high ability to inhibit HMGR by competitive inhibition with respect to (S)-3-hydroxy-3-methylglutaryl-CoA
small heterodimer partner nuclear receptor
-
directly regulates cholesterol biosynthesis through inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase
-
SMase C
-
treatment of fibroblasts with SMase C results in a 90% inhibition of HMGCR
-
sodium (E,3R,5S)-7-(2-(2-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
has almost no effect on the activity
sodium (E,3R,5S)-7-(2-(3-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
-
sodium (E,3R,5S)-7-(2-(4-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
shows the most potent inhibitory activity among compounds comparable with that of clinically useful mevastatin
sodium (E,3R,5S)-7-(2-phenyl-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoate
-
has almost no effect on the activity
sodium (E,3R,5S)-7-(4-(3-(2-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
sodium (E,3R,5S)-7-(4-(3-(3-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
sodium (E,3R,5S)-7-(4-(3-phenylpentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
atorvastatin
-
has a differentiating effect on wild-type and mutant forms of the human protein
atorvastatin
inhibits the cell growth as well as the activity of recombinant enzyme, 315.5 nM are enough to cause 50% recombinant LdHMGR enzyme inhibition, 93.2% inhibition at 0.001 mM
cerivastatin
-
biphasic inhibition mechanism, slow, tight-binding type of inhibitor
cycloheximide
-
downregulation of protein synthesis, synergistic with eicosapentanoic acid and myristic acid
fluvastatin
-
has a differentiating effect on wild-type and mutant forms of the human protein
GFPTGG
-
HMG-CoA competitive inhibitor; NADPH and HMG-CoA competitive inhibitor
GFPTGG
-
competitive, effects on enzyme Michaelis-Menten kinetics, overview
lovastatin
-
no effect of lovastatin on the growth curve of Hortaea werneckii in salt-free media, whereas remarkably reduced growth in the otherwise physiologically optimal medium containing 17% NaCl, an effect even more pronounced in hypersaline medium containing 25% NaCl. Inhibition of HMGR in vivo by lovastatin impairs the halotolerant character
lovastatin
-
the representative of the statin class of drugs that in their active hydrolysed form are specific inhibitors of the enzyme
lovastatin
-
slightly inhibitory statin for class II enzyme, binding structure at the active site involves the residues Lys267, Asn271, Glu83, Arg261, and 2 water molecules, substrate mimicking binding mode
lovastatin
-
competitive inhibitor for HMG-CoA binding site and noncompetitive inhibitor for NADPH binding site
pravastatin
inhibitory in the presence of increasing concentrations of NADPH, but increasing concentrations of HMG-CoA block the HMG-CoA reductase-inhibiting activity
rosuvastatin
-
thermodynamics of binding and inhibition mechanism, Glu559 is involved, reversible, 2-step complex formation, competitive with respect to 3-hydroxy-3-methylglutaryl-CoA, non-competitive to NADPH
simvastatin
-
does not allow differentiation between the wild-type and mutant forms of the human protein
simvastatin
inhibits the cell growth as well as the activity of recombinant enzyme, 63% inhibition at 0.1 mM
simvastatin
-
enzyme inhibition causes 40% reduction of wound healing, inhibition of HMGR activity during acute wound healing interferes with keratinocyte VEGF production and proliferation at the wound site, overview
additional information
-
whether plants are grown with mevalonate from the beginning or only during the last 9 days, HMGR activity is drastically reduced to 25% of the activity in plants grown in the absence of mevalonate. Plants grown without mevalonate during the last 9 days show a severe, though less pronounced, reduction in HMGR activity, which decreases to 60% of the activity in control plants. Significant reduction of HMGR activity does not correlate with changes in both the expression of HMG1 and HMG2 genes and the amount of HMGR protein
-
additional information
no inhibition by farnesoate and farnesoic acid
-
additional information
no inhibition by farnesoate and farnesoic acid
-
additional information
-
27-hydroxycholesterol strongly supresses the expression of HMGR, the in vivo inhibition of sterol 27-hydroxylase CYP27A1, e.g. by the drugs rapamycin and cyclosporine A, reduces the inhibition and thus increases HMGR activity, overview
-
additional information
screening of eight-membered medium ring lactams and related tricyclic compounds, either seven-membered lactams, thiolactams or amines, for inhibitory potency, overview. The compounds are inhibitory also in the presence of increasing concentrations of NADPH, and are not affected by increasing concentrations of HMG-CoA. Medium ring lactams and existing statins may have different mechanisms of enzyme interaction and inhibition, molecular docking studies and comparisons using the HMG-CoA reductase statin-binding receptor model, overview. The ligands may occupy a narrow channel housing the pyridinium moiety on NADP+
-
additional information
-
screening of eight-membered medium ring lactams and related tricyclic compounds, either seven-membered lactams, thiolactams or amines, for inhibitory potency, overview. The compounds are inhibitory also in the presence of increasing concentrations of NADPH, and are not affected by increasing concentrations of HMG-CoA. Medium ring lactams and existing statins may have different mechanisms of enzyme interaction and inhibition, molecular docking studies and comparisons using the HMG-CoA reductase statin-binding receptor model, overview. The ligands may occupy a narrow channel housing the pyridinium moiety on NADP+
-
additional information
-
methanolic extracts of Quercus infectoria galls, Rosa damascena flowers, and Myrtus communis leaves inhibit the enzyme activity noncompetitively to 84%, 70%, and 62%, respectively. Extracts of diverse other plants are also inhibitory for the enzyme, detailed overview
-
additional information
statins are potent enzyme inhibitors that bind to the active site where also the natural substrate binds, used widely in the treatment of hypercholesterolemia
-
additional information
-
design of highly potent and competitive inhibitory peptides for 3-hydroxy-3-methylglutaryl CoA reductase, no inhibition with SFGYVAG peptide
-
additional information
-
the activity of microsomal isoyzme Hmg2 is highest under hypo-saline and extremely hyper-saline conditions, and down-regulated under optimal growth conditions
-
additional information
exogenous supplementation of ergosterol in case of atorvastatin and resveratrol treated cells causes complete reversal of growth inhibition whereas simvastatin is ergosterol refractory
-
additional information
-
exogenous supplementation of ergosterol in case of atorvastatin and resveratrol treated cells causes complete reversal of growth inhibition whereas simvastatin is ergosterol refractory
-
additional information
-
inhibition potency of inhibitors in hepatocytes, myocytes and on purified enzyme, overview
-
additional information
-
no inhibition by geraniol or by its glucoside and thioglucoside
-
additional information
-
discovery, synthesis, and optimization of substituted pyrrole-based hepatoselective ligands as potent inhibitors of HMG-CoA reductase for reducing low density lipoprotein cholesterol (LDL-c) in the treatment of hypercholesterolemia
-
additional information
-
design, synthesis and evaluation of structure-based peptide inhibitors, computational methods, overview
-
additional information
-
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoic acid shows no apparent HMGR inhibitory activity even at 100 mM
-
additional information
-
the hybrid is resistant to race 0 of Phytophtora infestans
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
myristic acid
-
stimulates translation of the enzyme about 1.8fold at 0.15 mM, upregulation
squalestatin
-
leads to a significant concentration-dependent activation of HMGR of ca. 3fold the activity in untreated plants. Maximal HMGR activation at 0.06 mM squalestatin. No relevant changes in the level of expression of the HMG genes or in the amount of HMGR protein
supernatant protein factor
-
i.e. SPF, a 46 kDa cytosolic protein, stimulation of squalene monooxygenase and cholesterol biosynthesis in hepatoma cell culture, acts directly on the enzyme, not by increasing the enzyme amount
-
terbinafine
-
leads to a significant concentration-dependent activation of HMGR of ca. 3fold the activity in untreated plants. Maximal HMGR activation at 0.75 mM terbinafine. No relevant changes in the level of expression of the HMG genes or in the amount of HMGR protein
additional information
-
leaf tissue of Artemisia annua transgenic lines possess significantly higher HMGR activity compared with wild-type controls, and this activity is associated exclusively with microsomal membranes and with higher artemisinin content (increase of up to 22.5% artemisin in content compared with wild-type control Artemisia annua plants)
-
additional information
-
phosphorylation of HMGCR is stimulated by SMase C or exogenous ceramide
-
additional information
-
the activity of microsomal isoyzme Hmg2 is highest under hypo-saline and extremely hyper-saline conditions, and down-regulated under optimal growth conditions
-
additional information
-
4fold enzyme induction by root cutting within 2 h, and strong induction by infection with Phytophtora infestans, maximal 66fold after 2 h, induction mechanism
-
additional information
-
about 40fold enzyme induction by root cutting within 14 h, and about 875fold induction by infection with Phytophtora infestans after 22 h, induction mechanism
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
(R)-mevaldehyde
pH 7.3, 37°C, second step of the reaction, mutant enzyme 404N with Asp is added at position 404
0.032
(R)-mevaldehyde
pH 7.3, 37°C, second step of the reaction, wild-type enzyme
0.084
(R)-mevaldehyde
pH 7.3, 37°C, second step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404
0.1
(R)-mevaldehyde
pH 7.3, 37°C, second step of the reaction, mutant enzyme H398Q
0.0017
(R)-mevalonate
-
mutant enzyme L403R/G404R/A406S, at pH 9.0 and 50°C
0.06
(S)-3-hydroxy-3-methylglutaryl-CoA
pH 7.3, 37°C, first step of the reaction, wild-type enzyme
0.077
(S)-3-hydroxy-3-methylglutaryl-CoA
pH 7.3, 37°C, first step of the reaction, mutant enzyme 404N with Asp is added at position 404
0.083
(S)-3-hydroxy-3-methylglutaryl-CoA
pH 7.3, 37°C, first step of the reaction, mutant enzyme 404D with Asp is added at position 404
0.083
(S)-3-hydroxy-3-methylglutaryl-CoA
pH 7.3, 37°C, first step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404
0.2
(S)-3-hydroxy-3-methylglutaryl-CoA
pH 7.3, 37°C, first step of the reaction, mutant enzyme H398Q
0.014
3-hydroxy-3-methylglutaryl-CoA
-
reductase from liver and reductase from tumor
0.6
3-hydroxy-3-methylglutaryl-CoA
-
pH 7.5, temperature not specified in the publication
0.03
NADPH
-
pH 6.5, 37°C, (S)-3-hydroxy-3-methylglutaryl-CoA reduction
0.066
NADPH
pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, wild-type enzyme
0.068
NADPH
pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404D with Asp is added at position 404
0.068
NADPH
pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404
0.072
NADPH
pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404N with Asp is added at position 404
0.177
NADPH
pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme H398Q
0.55
NADPH
pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, wild-type enzyme
2.1
NADPH
pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404
3
NADPH
pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme H398Q
4.2
NADPH
pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme 404N with Asp is added at position 404
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.027
fluvastatin
-
pH 6.8, 25°C, versus (S)-3-hydroxy-3-methylglutaryl-CoA
additional information
additional information
-
steady state inhibition kinetics
-
additional information
additional information
-
inhibition kinetics of different plant extracts, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000035
(3R,5R)-7-(1-ethyl-3-(4-fluorophenyl)-4-methyl-5-[(5-methyl-pyrazin-2-ylmethyl)-carbamoyl]-1H-pyrrol-2-yl)-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000029
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-4-methyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000024
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxybenzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000028
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxycarbonyl-benzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000017
(3R,5R)-7-[3-(4-fluoro-phenyl)-1-isopropyl-5-phenylcarbamoyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000043
(3R,5R)-7-[3-(4-fluorophenyl)-1-isopropyl-4-phenyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000018
(3R,5R)-7-[3-(4-fluorophenyl)-5-[(3-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000007
(3R,5R)-7-[3-(4-fluorophenyl)-5-[[4-(methoxymethyl)benzyl]carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.00000011
(3R,5R)-7-[5-(4-carboxy-benzylcarbamoyl)-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid disodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000015
(3R,5R)-7-[5-benzylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid
Rattus norvegicus
-
37°C, hepatocytes
0.000032
(3R,5R)-7-[5-carbamoyl-1-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000049
(3R,5R)-7-[5-carbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000021
(3R,5R)-7-[5-cyano-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000012
(3R,5R)-7-[5-[(3-carbamoylbenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000002
(3R,5R)-7-[5-[(4-cyanobenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000012
(3R,5R)-7-[5-[[4-(dimethylcarbamoyl)benzyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
2.2 - 26
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
0.0000022
4-[[([5-[(3R,5R)-6-carboxy-3,5-dihydroxyhexyl]-4-(4-fluorophenyl)-1-(1-methylethyl)-3-phenyl-1H-pyrrol-2-yl]carbonyl)amino]methyl]benzoic acid
Mus musculus
-
inhibition of purified enzyme
0.0000018
7-[3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000007
7-[3,4-bis(4-fluorophenyl)-5-[(3-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000066
7-[3,4-bis(4-fluorophenyl)-5-[(3-methoxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000124
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.000015
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(propylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000029
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(4-sulfamoylphenyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000008
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(pyridin-2-ylmethyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000015
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(4-methyl-1,3-thiazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000034
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-imidazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000026
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-pyrazol-3-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000088
7-[3-(4-fluorophenyl)-5-(methylcarbamoyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000004
7-[3-(4-fluorophenyl)-5-[(4-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000008
7-[3-(4-fluorophenyl)-5-[(4-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000008
7-[5-(benzylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000038
7-[5-(cyclopropylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.00002
7-[5-(dimethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.000012
7-[5-(ethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.000003
7-[5-carbamoyl-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000051
7-[5-ethylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000003
7-[5-[(4-carbamoylphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000003
7-[5-[(4-carboxyphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000006
7-[5-[[(1,5-dimethyl-1H-pyrazol-3-yl)methyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000003
7-[5-[[3-(dimethylcarbamoyl)phenyl]carbamoyl]-3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000014
7-[5-[[4-(dimethylcarbamoyl)phenyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.201
Ile-Ala-Val-Pro-Gly-Glu-Val-Ala
Homo sapiens
-
pH and temperature not specified in the publication
0.04265
methyl (2-methoxy-5-nitro-4-propylphenoxy)acetate
[Candida] glabrata
-
at pH 8.0 and 37°C
0.04
mevastatin
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.82
sodium (E,3R,5S)-7-(2-(2-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
1.2
sodium (E,3R,5S)-7-(2-(3-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.15
sodium (E,3R,5S)-7-(2-(4-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.85
sodium (E,3R,5S)-7-(2-phenyl-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
7.4
sodium (E,3R,5S)-7-(4-(3-(2-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
92
sodium (E,3R,5S)-7-(4-(3-(3-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (3.7 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
1.8
sodium (E,3R,5S)-7-(4-(3-phenylpentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
2.2
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
26
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (3.7 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.003
fluvastatin
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01333
mutant enzyme S577A from transgenic line 2, at 30°C, pH not specified in the publication
0.01644
mutant enzyme S577A from transgenic line 1, at 30°C, pH not specified in the publication
0.01949
wild type enzyme from transgenic line 1, at 30°C, pH not specified in the publication
0.03568
wild type enzyme from transgenic line 2, at 30°C, not pH not specified in the publication
4.9
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.8
7.2
7.3
7.4
7.5
9.5
additional information
additional information
-
two pH optima are found, corresponding to HMGR from the heavy or the light fractions: pH 7.0 and pH 75, respectively
additional information
-
two pH optima are found, corresponding to HMGR from the heavy or the light fractions: pH 7.9 and pH 6.9, respectively
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
dual-function enzyme with acetoacetyl-coenzyme A thiolase and 3-hydroxy-3-methylglutaryl-coenzyme A reductase activities
-
-
brenda
clone RY8813 at the Experimental Farm of the Chinese Academy of Tropical Agriculture Science
-
-
brenda
lobster, 2 enzyme forms: a soluble and a membrane-bound enzyme
SwissProt
brenda
lobster, 2 enzyme forms: a soluble isozyme HMGR1 and a membrane-bound isozyme HMGR2
SwissProt
brenda
salt-tolerant black yeast, strain MZKI B736, isozymes Hmg1 and Hmg2
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
strong expression of isoform HMGR2 in female strobili, lowest expression of isoform HMGR2 in male strobili
brenda
-
genes LcHMG1 and LcHMG2 exhibit distinct expression patterns during litchi fruit development. LcHMG1 expression is highest in the early stage of fruit development, correlated with the high level of cell division. Absolute levels of LcHMG1 expression vary among fruits of different pheno- or genotypes, with expression in large-fruited types reaching higher levels for longer duration compared to that in small-fruited types. LcHMG2 is most highly expressed in the late stage of fruit development, in association with biosynthesis of isoprenoid compounds required for later cell enlargement
brenda
-
NCTC 2544 cells. HMG-CoA reductase and peroxisome proliferator-activated receptor alpha are involved in clofibrate-induced apoptosis in human keratinocytes
brenda
strongest expression of isoform HMGR3 in leaves
brenda
-
-
brenda
-
HMG-CoA reductase activity is higher in both female and male Nagase analbumimetic rats than in Sprague-Dwwley rats. Ovariectomy results in no significant changes in total hepatic HMG-CoA reductase in female Sprague-Dawley rats
brenda
-
modified HMG-CoA reductase and low density lipoprotein receptor regulation is deeply involved in age-related hypercholesterolemia
brenda
-
the enzyme is fully activated both in acute and in chronic thioacetamide-treated animals, while no modifications are detected in its KM and in its short-term regulatory enzymes
brenda
-
HMG-CoA reductase activity is higher in both female and male Nagase analbumimetic rats than in Sprague-Dwwley rats. Ovariectomy results in no significant changes in total hepatic HMG-CoA reductase in female Sprague-Dawley rats
-
brenda
-
modified HMG-CoA reductase and low density lipoprotein receptor regulation is deeply involved in age-related hypercholesterolemia
-
brenda
additional information
the enzyme shows a strong expression in nodes followed by leaves and stem. Roots record the lowest expression level among all the tissues tested
brenda
additional information
-
the enzyme shows a strong expression in nodes followed by leaves and stem. Roots record the lowest expression level among all the tissues tested
brenda
additional information
-
growth at high and low salinity, quantitative expression analysis, overview, the expression of HMGR is regulated in response to non-optimal salinity in the halophilic archaeon
brenda
additional information
very low content in other tissues, higher enzyme activity in male organisms than in female, tissue distribution overview
brenda
additional information
very low content in other tissues, higher enzyme activity in male organisms than in female, tissue distribution overview
brenda
additional information
-
very low content in other tissues, higher enzyme activity in male organisms than in female, tissue distribution overview
brenda
additional information
-
the activity of microsomal isoyzme Hmg2 is highest under hypo-saline and extremely hyper-saline conditions, and down-regulated under optimal growth conditions, while the activity of the truncated mitochondrial Hmg1 is constant under different growth conditions
brenda
additional information
-
analysis of LcHMG1 and LcHMG2 expressions in various litchi tissues, developmental stages and genotypes, overview. Expression of LcHMG1 and LcHMG2 is universally detected in all the tissues analyzed, including unfertilized female flowers, fruit tissues, leaves, shoots, and roots but their expression level appears to vary from tissue to tissue, with the highest expression found in the young pericarp (39 DAA) and the lowest in the aged seed. High level of expression in young tissues compared to aged tissues for a given organ except root
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme undergoes endoplasmic reticulum-associated degradation which is physiologically regulated by sterol pathway signals
-
brenda
-
localized predominantly within spherical vesicular structures that range from 0.0002-0.0006 mm in diameter, located in the cytoplasm and within the central vacuole in differentiated cotyledon cells. The N-terminal region, including the transmembrane domain of HMGR, is found to be necessary and sufficient for directing HMGR to the endoplasmic reticulum and the spherical structures
brenda
-
located on the cytoplasmic site, integrated into the membrane
brenda
-
the enzyme spans the endoplasmic reticulum membrane twice. Both the N-terminal region and the highly conserved catalytic domain are in the cytosol, whereas only a short stretch of the protein is in the endoplasmic reticulum lumen. Insertion in the endoplasmic reticulum membrane is mediated by the signal recognition particle (SRP) that recognizes the two hydrophobic sequences which will become membrane spanning segments
brenda
bound, isozyme HMGR2, about 25% of total enzyme content
brenda
-
the HMGR activity is detected in the final microsomal pellet after ultracentrifugation
-
brenda
-
-
-
brenda
isozyme HMGR1, about 75% of total enzyme content
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
Ochromonas malhamensis
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
malfunction
-
inhibition of enzyme expression promotes the accumulation of anthocyanins and fruit coloration
malfunction
the enzyme is important in the biosynthesis of terpenoids such as patchouli alcohol
metabolism
HMG-CoA reductase is the rate-limiting enzyme of cholesterol biosynthesis
metabolism
-
HMGR catalyzes the first committed step in mevalonic acid pathway for biosynthesis of isoprenoids
metabolism
HMGR catalyzes the four-electron reduction of HMGCoA to mevalonate, the committed step in the biosynthesis of sterols. Mevalonate is a precursor of isoprenoids, a class of compounds involved in several cellular functions such as cholesterol synthesis and growth control
metabolism
-
3-hydroxy-3-methylglutaryl Co-A reductase is a rate-limiting enzyme in the eukaryotic mevalonate pathway
metabolism
-
3-hydroxy-3-methylglutaryl CoA reductase catalyzes the first committed step in the mevalonic acid (MVA) pathway for the biosynthesis of isoprenoids
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
Ochromonas malhamensis
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
rate limiting enzyme of the ergosterol biosynthetic pathway
metabolism
the enzyme a key enzyme in the synthetic pathway of protostane triterpenes, including Alisol B 23-acetate and its derivatives
metabolism
enzyme overexpression significantly increases abscisic acid, gibberellic acid, carotene, and lycopene content, indicating that the enzyme participates in the regulation of terpenoid compound synthesis
metabolism
rate-limiting enzyme in mammalian phosphatidylethanolamine biosynthesis
metabolism
rate-limiting enzyme in mammalian phosphatidylethanolamine biosynthesis
metabolism
-
3-hydroxy-3-methylglutaryl Co-A reductase is a rate-limiting enzyme in the eukaryotic mevalonate pathway
-
metabolism
-
rate limiting enzyme of the ergosterol biosynthetic pathway
-
physiological function
within cells, the concentration of mevalonate and therefore that of its metabolic products is tightly controlled through the activity of HMGR, an enzyme that catalyzes the four-electron reduction of 3-hydroxy-3-methylglutaryl-CoA to mevalonate
physiological function
-
HMG1 is highly associated with the cell division during the early stage of fruit development which determines the final fruit size in Litchi chinensis. LcHMG2 is involved in the late stage of fruit development, in association with biosynthesis of isoprenoid compounds required for later cell enlargement
physiological function
rate-limiting enzyme for cholesterol synthesis, regulated via a negative feedback mechanism through sterols and non-sterol metabolites derived from mevalonate
physiological function
-
the enzyme is the major regulatory enzyme of cholesterol biosynthesis and the target enzyme of many investigations aimed at lowering the rate of cholesterol biosynthesis
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
Ochromonas malhamensis
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated. Protein phosphatase 2A (PP2A) is both a transcriptional and a posttranslational regulator of HMGR in Arabidopsis thaliana
physiological function
the enzyme plays an important role in catalyzing the first committed step of isoprenoid biosynthesis in the mevalonic acid pathway catalyzing the conversion of HMG-CoA to mevalonic acid in plants
physiological function
-
brassinosteroids inhibit enzyme activity and cooperate with the enzyme to regulate the formation of color, aroma, and other quality characteristics in fruits
physiological function
-
overexpression of isoform HMGR5 enhances tolerance to oxidative stress by maintaining photosynthesis and scavenging reactive oxygen species in transgenic Arabidopsis thaliana
additional information
modelling of the active site using crystal stucture of the enzyme with bound inhibitor simvastatin, PDB ID 1HW9, overview
additional information
structure-function analysis, overview. Identification of three characteristic sites of hydroxymethylglutaryl-CoA reductase
additional information
-
structure-function analysis, overview. Identification of three characteristic sites of hydroxymethylglutaryl-CoA reductase
additional information
devlopment of three molecular models of human enzyme with different active site protonation states, and reaction mechanism analysis by molecular dynamics and quantum mechanics/molecular mechanics (QM/MM) calculations to detail the first reduction step, the rate-limiting step, of HMG-CoA-R
additional information
structure-function analysis of HMGR, homology modelling using human HMGR, PDB ID 1DQ8A, as template, overview
additional information
-
structure-function analysis of HMGR, homology modelling using human HMGR, PDB ID 1DQ8A, as template, overview
Show AA Sequence and Transmembrane Helices (8294 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
11000
46000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
oligomer
1 x 69000, recombinant His-tagged isozyme HMGR1, SDS-PAGE
tetramer
additional information
?
x * 64600, about, sequence calculation, x * 66500, recombinant enzyme, SDS-PAGE
?
x * 61500, isoform HMGR3, calculated from amino acid sequence
?
x * 61700, isoform HMGR2, calculated from amino acid sequence
dimer
the catalytic portion of human HMG-CoA, after cleavage of the probable dimeric form found in the endoplasmic reticulum, 18 crystallized as a dimer of dimers. However, the dimer-dimer interface is distant from the active site and only the dimer of the molecule seems crucial for catalysis
additional information
tertiary structure modelling, overview
additional information
-
tertiary structure modelling, overview
additional information
-
JcHMGR has three domains: 1. the small, helical N-terminal N-domain, 2. the large, central L-domain harboring two HMG-CoA binding motifs EMPIGFLQIP and TTEGCLVA, and an NADP(H)-binding motif GTVGGGT, and 3. the small helical S-domain harboring an NADP(H)-binding motif characterized by the sequence DAMGMN
additional information
the secondary structure of LdHMGR confirms the presence of 25.7% alpha helicity
additional information
-
the secondary structure of LdHMGR confirms the presence of 25.7% alpha helicity
additional information
-
the secondary structure of LdHMGR confirms the presence of 25.7% alpha helicity
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
lipoprotein
identification of nineteen N-myristoylation sites and three characteristic sites
phosphoprotein
proteolytic modification
-
proteolysis releases a soluble, active fragment of 52-56 kDa
additional information
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
isoform HMGR1S is inactivated through phosphorylation at Ser577 by the AKIN10-GRIK1 kinase cascade system in vitro
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
the enzyme is phosphorylated at Ser872 by AMP-activated protein kinase and reversibly dephosphorylated by phosphatase 2A
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
Ochromonas malhamensis
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
-
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
identification of a cAMP-and cGMP-dependent protein kinase phosphorylation site, thirteen Protein kinase C phosphorylation sites, and eleven Casein kinase II phosphorylation sites
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
the isozyme is not regulated by phosphorylation
additional information
the isozyme is not regulated by phosphorylation
additional information
the isozyme is probably not regulated by phosphorylation
additional information
the isozyme is probably not regulated by phosphorylation
additional information
-
the isozyme is probably not regulated by phosphorylation
additional information
-
genistein, eicosapentaenoic acid and docosahexaenoic acid down-regulate reductase activity, primarily through posttranscriptional effects
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
ubiquitination and proteasomal degradation of microsomal, but not mitochondrial, HMGR isozymes depends on environmental salinity, overview
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
Ochromonas malhamensis
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the enzyme crystal structure (PDV ID 1DQA) at 2.0 A resolution
enzyme in complex with inhibitor lovastatin, from 1.2 M ammonium sulfate, at 20°C, a few days, larger crystals by microseeding, complexing with the inhibitor by soaking in a KOH solution, pH 9.0, containing 2 mM lovastatin, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S577A
the mutant shows reduced activity compared to the wild type enzyme
A333P
mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation
G87R
mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation
S60N
mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation
H398Q
Q766H
-
restores viability of Saccharomyces cerevisiae strains lacking the HMG1 and HMG2 genes, thus is catalytically active in yeast cells. Q766H mutation, which affects the structure of the catalytic domain, increases the sensitivity of the enzyme towards statin treatment
R393Q
-
restores viability of Saccharomyces cerevisiae strains lacking the HMG1 and HMG2 genes, thus is catalytically active in yeast cells. R393Q mutation does not change the properties of the enzyme towards statin treatment
S872D
the mutation reduces the catalytic activity of the enzyme similarly to that of the phosphorylated enzyme
L403R/G404R/A406S
synthesis
-
due to use of rare codon, expression of enzyme in Escherichia coli is poor. Coexpression of the S. solfataricus hmgA gene with the argU gene that encodes tRNAAGA,AGG resulted in an over 10-fold increase in enzyme yield
additional information
H398Q
low activity for catalysis of reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA or oxidative acylation of mevaldehyde, but readily catalyzed mevaldehyde reduction
H398Q
-
low activity for catalysis of reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA or oxidative acylation of mevaldehyde, but readily catalyzed mevaldehyde reduction
-
L403R/G404R/A406S
-
engineering of an appropriately located phosphoacceptor serine and cAMP-dependent protein kinase recognition motif to create a phosphorylation site. Km values, Vmax, optimal pH and temperature of mutant are identical to wild-type. Exposure of mutant to ATP and cAMP-dependent protein kinase is accompanied by incorporation of phosphate and by a parallel decrease in catalytic activity. Subsequent treatment with a protein phosphatase releases enzyme-bound 32Pi and restores activity to pretreatment levels
additional information
-
construction of insertion mutants of the 2 isozymes leads to loss of enzyme function, the hmg1 mutant plants show an altered phenotype with dwarfing, early senescence, male sterility, and both mutants of hmg1 and hmg2 show reduced sterol levels, the mutants are more sensitive to the inhibitor lovastatin and squalestatin, overview
additional information
-
transgenic expression of the N-terminal truncated 3-hydroxy-3-methylglutaryl CoA reductase from Arabidopsis thaliana in Lavandula latifolia plants enhances production of essential oils and sterols in the different lines of transgenic plants, expression of HMGR1S also increases the amount of the end-product sterols beta-sitosterol and stigmasterol by 1.8fold and 1.9fold, respectively, but does not affect the accumulation of carotenoids or chlorophylls, overview
additional information
mutant forms of the 403 residue Haloferax volcanii enzyme are constructed to model phosphorylation and infer whether attenuated activity involves interaction with His398. Chimeric Haloferax volcanii-hamster enzymes constructed in an effort to create an active, phosphorylatable chimeric enzyme are inactive or not phosphorylated. Asp is added at position 404 to mimic the introduction of negative charge that would accompany phosphorylation. Enzyme 404D/H398Q was inactive for reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA or oxidative acylation of mevaldehyde, but catalyzed reaction mevaldehyde reduction at 35% the wild-type rate. These observations are consistent with the model that attenuation of catalytic activity results from an ionic interaction between the imidazolium cation of His 398 and the carboxylate anion of Asp404
additional information
-
mutant forms of the 403 residue Haloferax volcanii enzyme are constructed to model phosphorylation and infer whether attenuated activity involves interaction with His398. Chimeric Haloferax volcanii-hamster enzymes constructed in an effort to create an active, phosphorylatable chimeric enzyme are inactive or not phosphorylated. Asp is added at position 404 to mimic the introduction of negative charge that would accompany phosphorylation. Enzyme 404D/H398Q was inactive for reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA or oxidative acylation of mevaldehyde, but catalyzed reaction mevaldehyde reduction at 35% the wild-type rate. These observations are consistent with the model that attenuation of catalytic activity results from an ionic interaction between the imidazolium cation of His 398 and the carboxylate anion of Asp404
additional information
-
mutant forms of the 403 residue Haloferax volcanii enzyme are constructed to model phosphorylation and infer whether attenuated activity involves interaction with His398. Chimeric Haloferax volcanii-hamster enzymes constructed in an effort to create an active, phosphorylatable chimeric enzyme are inactive or not phosphorylated. Asp is added at position 404 to mimic the introduction of negative charge that would accompany phosphorylation. Enzyme 404D/H398Q was inactive for reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA or oxidative acylation of mevaldehyde, but catalyzed reaction mevaldehyde reduction at 35% the wild-type rate. These observations are consistent with the model that attenuation of catalytic activity results from an ionic interaction between the imidazolium cation of His 398 and the carboxylate anion of Asp404
-
additional information
-
coexpression of N-terminal truncated Hevea brasiliensis (S)-3-hydroxy-3-methylglutaryl CoA reductase and tobacco C24-sterol methyltransferase type 1 in transgenic Nicotiana tabacum plants enhances carbon flux towards end-product sterols, expression under control of both seed-specific and constitutive promotors leads to enhancement of sterol accumulation by 2.5 and 2.1fold, respectively, analysis of the sterol spectrum, overview
additional information
-
expression of human HMG-CoA reductase in yeast complements the lethal phenotype of Saccharomyces cerevisiae strains lacking the HMG1 and HMG2 genes
additional information
identification of five single nucleotide polymorphisms, three of them are synonymous mutations and the other two are missense mutations, the naturally occuring mutation T1541C causes a deletion of a CdxA element and a C/EBP binding site and created a c-Ets-binding site, and naturally occuring mutation G973T in exon 9, which is a synonymous mutation
additional information
-
identification of five single nucleotide polymorphisms, three of them are synonymous mutations and the other two are missense mutations, the naturally occuring mutation T1541C causes a deletion of a CdxA element and a C/EBP binding site and created a c-Ets-binding site, and naturally occuring mutation G973T in exon 9, which is a synonymous mutation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19
-
below 19°C reversible inactivation of enzyme activity, prevented by NADPH and NADP+
90
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol strongly stabilizes the enzyme, stabilization against endoplasmic reticulum-associated degradation
-
presence of reduced thiol compounds is important for enzyme stability
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dithiothreitol
-
10 mM at pH 7 reverses CoA disulfide inactivation of enzyme
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Ochromonas malhamensis
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
-
740956
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, after quick freezing in acetone/solid CO2 at -80°C, one week, 10% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4380fold to homogeneity from microsomes by solubilization with trypsin, and affinity chromatography on 2',5'-ADP-resin and HMG-CoA-hexane resin
-
native soluble isozyme HMGR1 from mandibular organ by ultracentrifugation, anion exchange chromatography, ultrafiltration and gel filtration, recombinant enzyme from Sf9 insect cells by nickel affinity chromatography
Ni-NTA column chromatography
partially, preparation of microsomes and solubilization by trypsin
-
recombinant His-tagged catalytic domain from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli by nickel-affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant solubilized enzyme from Escherichia coli strain BL21(DE3) Rosetta by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a truncated protein is expressed in Escherichia coli BL21(DE3) cells
a truncated version of the protein lacking the N-terminal 249-bp GC rich area is expressed in Escherichia coli BL21(DE3) cells
-
cDNA encoding the wild-type and mutant forms of human HMG-CoA reductase expressed under control of the yeast MET25 promoter in a Saccharomyces cerevisiae strain with deletions of both HMG1 and HMG2
-
coexpression of the Sulfolobus solfataricus hmgA gene in Escherichia coli with the argU gene that encodes tRNAAGA,AGG results in an over 10fold increase in enzyme yield
-
construction of a N-terminally truncated enzyme, comprising the catalytic site, and subcloning into Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparisons, RT-PCR and real-time PCR expression analysis
DNA and amino aid sequence determination and analysis, cloning in Escherichia coli and functional complementation of a HMGR-deficient mutant yeast strain using the yeast-Escherichia coli coli shuttle vector pYF1845
expression in Escherichia coli
expression of c-myc-tagged enzyme from plasmid in yeast, expression as GFP-fusion protein
-
expression of the His-tagged catalytic domain of the enzyme, residues E416-F887, in Escherichia coli
-
functional complementation of EuHMGR in HMGR-deficient mutant yeast JRY2394 demonstrates that EuHMGR mediates the mevalonate biosynthesis in yeast
gene HMGR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression in Escherichia coli strain BL21(DE3) Rosetta, quantitative realtime-PCR enzyme expression analysis
gene HMGR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, subcloning in Escherichia coli strain DH5alpha
gene HMGR, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene hmgR, expression analysis under different salinity growth conditions, hmgR transcript increases in abundance with increasing salinity by a factor of 2.2fold
-
gene hmgr, genomic DNA sequence and full-length cDNA, as well as JcHMGR amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain Top 10F'
-
genes LcHMG1 and LcHMG2, DNA and amino acid sequence determination and analysis, real-time quantitative RT-PCR expression analysis
-
isozyme HMGR1, DNA and amino acid sequence determination and analysis, functional expression in Spodoptera frugiperda Sf9 cells via baculovirus infection system as His-tagged enzyme
isozyme HMGR2, DNA and amino acid sequence determination and analysis
overexpression in Escherichia coli
overexpression of the HMGR gene in transgenic Artemisia annua plants using Agrobacterium-mediated gene transfer technology
-
overexpression of the recombinant His-tagged enzyme in Lactococcus lactis strain NZ9000, co-expression with sesquiterpene synthase gene, PMSTS from Persicaria minor incorporated into the pNZ8048 plasmid, with two base substitutions, 796A.G and 1077A.G, introduced into the PMSTS gene during amplification resulting in exchange K266E and a silent mutation
-
the HMG1-overexpressing episome (pRS434GAP-HMG1) introduced into 36 type strains purchased from ATCC, and yeast recombinant AURGG101
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after oxidative stress treatment with 0.1 mM methyl viologen, the expression level of isoform HMGR5 is up-regulated significantly at 24 h
-
at 8 h after cold treatment, the transcription level of isoform HMGR3 sharply increases to a peak value that is 4.5fold that of the control. Isoform HMGR3 expression reaches the maximum value, which is 1.67fold that of the control at 4 days after treatment with methyl jasmonate. Abscisic acid treatment shows similarly increasing values until a moderate peak at 2 days after treatment. Salicylic acid and ethanol treatments distinctly upregulated the expression of isoform HMGR3 with the peak appearing at 5 days after treatment. The former increases the expression by 3.74fold and the latter by 34.6fold compared with that of the control
enzyme expression is increased 6 h after treatment with 0.2 mM abscisic acid, 6 h after treatment with 200 mM NaCl, 3 days after treatment with 10% (w/v) PEG 6000, 1 h after treatment with 2 mM H2O2, and 7 days after cold treatment at 4°C
expression of 3-hydroxy-3-metylglutaryl coenzyme A reductase is down-regulated by methyl jasmonate treatment
-
increased Hmgcr mRNA levels after serum starvation
increased Hmgcr mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
rubber yields and/or yield characteristics are significantly positively correlated with enzyme expression levels
the expression level of isoform HMGR3 is considerably downregulated under dark treatment, that is, 8% of the control at 24 h after treatment
the isoform HMGR2 expression is substantially depressed under dark treatment and is 90% lower than that of the control at 8 h after treatment. Methyl jasmonate treatment causes the continuous downregulation of isoform HMGR2 transcription level at 5% that of the control at 4 days after treatment. The expression level of isoform HMGR2 is downregulated in response to abscisic acid treatment, yielding a value 90% lower than that of the control at 5 days after treatment
under cold treatment, the isoform HMGR2 expression is enhanced by 6.6fold compared with that of the control, and reaches the highest level at 48 h. Under salicylic acid treatment, the expression level of isoform HMGR2 initially decreases first and then increases, and the value is 80% higher than that of the control at 3 days after treatment. Ethanol treatment induces the transcript of isoform HMGR2, which continually increases and reaches the highest expression value at 978% higher than that of the control at 4 days after treatment
increased Hmgcr mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
increased Hmgcr mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from inclusion bodies after expression in Escherichia coli strain BL21(DE3) Rosetta
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
overexpression of HMG1 is the most effective among all other genes in both hosts Saccharomyces cerevisiae ATCC 200589 and ATCC 76625 for prenyl alcohol production
drug development
medicine
molecular biology
nutrition
engineering of Yarrowia lipolytica for de novo production of the food and feed additive astaxanthin by fermentation. The astaxanthin-producing Yarrowia lipolytica shows great promise for employment in biological astaxanthin production. The genes for beta-carotene biosynthesis: bi-functional phytoene synthase/lycopene cyclase (crtYB) and phytoene desaturase (crtI) from Xanthophyllomyces dendrorhousa are introduced. The activities of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG1) and geranylgeranyl diphosphate synthase (GGS1/crtE) in the best producing strain are optimized. Downregulation of the competing squalene synthase SQS1 increases the beta-carotene titer. Then a beta-carotene ketolase (crtW) from Paracoccus sp. N81106 and hydroxylase (crtZ) from Pantoea ananatis are introduced to convert beta-carotene into astaxanthin. The constructed strain accumulates 10.4 mg/l of astaxanthin but also accumulates astaxanthin biosynthesis intermediates, 5.7 mg/l canthaxanthin, and 35.3 mg/l echinenone. The copy numbers of crtZ and crtW are optimized to obtain 3.5 mg/g dry cell weight (54.6 mg/l) of astaxanthin in a microtiter plate cultivation
drug development
-
inhibitors of HMG-CoA reductase for reducing low density lipoprotein cholesterol in the treatment of hypercholesterolemia
drug development
-
a yeast expression system can serve to study the influence of selected mutations in human HMG-CoA reductase on the sensitivity of the enzyme to commonly prescribed statins, thus this model system is suitable for the development and selection of lipid-lowering drugs as well as for the examination of DNA sequence variations in the context of statin therapy
drug development
-
overexpression of HMGR appears promising for obtaining a constant high production of artemisinin, an effective drug against malaria for which no resistant strains of Plasmodium falciparum have been reported
medicine
-
the enzyme is a target for intervention in the treatment of hypercholesterolaemia, clinical utility of inhibitors to decrease the levels of atherogenic lipiproteins in patients
medicine
-
dual therapy with the HMG-CoA reductase inhibitor pravastatin and the angiotensin receptor antagonist olmesartan, which produce an additive reduction in cardiomyocyte hypertrophy and cardiac fibrosis after myocardial infarction through different mechanisms, decreases the propensity of the heart to arrhythmogenesis
medicine
-
genistein, eicosapentaenoic acid and docosahexaenoic acid down-regulate reductase activity, primarily through posttranscriptional effects. Diets rich in soy isoflavones and fish oils, therefore, may exert anti-cancer effects through the inhibition of mevalonate synthesis in the breast. Genistein and docosahexaenoic acid, in particular, may augment the efficacy of statins, increasing the potential for use of these drugs in adjuvant therapy for breast cancer
medicine
the cholesterol absorption inhibitor ezetimibe profoundly lowers serum cholesterol levels in animals expressing very low rates of hepatic cholesterol synthesis and produces large compensatory increases in hepatic HMG-CoA reductase expression without signifucantly affecting expression of hepatic low density lipoprotein receptors. This indicates that ezitimibe should be most effective in lowering serum cholesterol levels in peaple with low rates of cholesterol synthesis/High rates of cholesterol absorption
medicine
-
treatment with the inhibitor atorvastatin exerts early nephroprotective effects in a rat model of chronic inhibition of nitric axide synthesis
molecular biology
-
Lactococcus lactis is a potential heterologous host for the production of sesquiterpenes from a herbaceous Malaysian plant, Persicaria minor. A sesquiterpene synthase gene encoding beta-sesquiphellandrene synthase from Persicaria minor is successfully cloned and expressed in Lactococcus lactis. Overexpression of the Lactococcus lactis endogenous 3-hydroxy-3-methylglutaryl Co-A reductase, an established rate-limiting enzyme in the eukaryotic mevalonate pathway, increases the production level of beta-sesquiphellandrene by 1.25-1.60 fold
molecular biology
-
Lactococcus lactis is a potential heterologous host for the production of sesquiterpenes from a herbaceous Malaysian plant, Persicaria minor. A sesquiterpene synthase gene encoding beta-sesquiphellandrene synthase from Persicaria minor is successfully cloned and expressed in Lactococcus lactis. Overexpression of the Lactococcus lactis endogenous 3-hydroxy-3-methylglutaryl Co-A reductase, an established rate-limiting enzyme in the eukaryotic mevalonate pathway, increases the production level of beta-sesquiphellandrene by 1.25-1.60 fold
-
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EXTERNAL LINKS (specific for EC-Number 1.1.1.34)
Transporter Classification Database (TCDB): 2.A.6.6.5, 2.A.6.6.10
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Release 2023.1 (January 2023)
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