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Information on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase
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EC Tree
1.1.1.30 3-hydroxybutyrate dehydrogenaseIUBMB Comments
Also oxidizes other 3-hydroxymonocarboxylic acids.
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Word Map
- 1.1.1.30
- ketone
- succinate
- acetoacetate
-
lipid-requiring
- lecithin
-
coa-transferase
- acetoacetyl-coa
- alpha-glycerophosphate
-
thiolase
-
3-oxoacid
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submitochondrial
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ketogenesis
-
enzyme-phospholipid
- analysis
- diagnostics
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
beta-hydroxybutyrate dehydrogenase, 3-hydroxybutyrate dehydrogenase, d-beta-hydroxybutyrate dehydrogenase, d-3-hydroxybutyrate dehydrogenase, beta-hydroxybutyric dehydrogenase, dhrs6, 3-hydroxybutyrate dehydrogenase-2, beta-hydroxybutyric acid dehydrogenase, 3-hbdh, 3hbdh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-D-hydroxybutyrate dehydrogenase
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3-HBDH
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3-hydroxybutyrate dehydrogenase
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3HBDH
BDH
BDH1
BDH2
BDH3
BdhA
beta-hydroxybutyrate dehydrogenase
beta-hydroxybutyric acid dehydrogenase
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beta-hydroxybutyric dehydrogenase
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D-(-)-3-hydroxybutyrate dehydrogenase
D-3-hydroxybutyrate dehydrogenase
D-beta-hydroxybutyrate dehydrogenase
HBD
HBDH
hydroxybutyrate oxidoreductase
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NAD-beta-hydroxybutyrate dehydrogenase
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Psyc_1428
additional information
BDH
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beta-hydroxybutyrate dehydrogenase
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D-(-)-3-hydroxybutyrate dehydrogenase
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D-3-hydroxybutyrate dehydrogenase
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D-beta-hydroxybutyrate dehydrogenase
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additional information
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the enzyme belongs to the family of short-chain dehydrogenases/reductases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
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(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
ordered Bi Bi mechanism, NAD+ first substrate, NADH last product to leave
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(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
enzyme is completely dependent on the presence of phospholipid for activity
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(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
the enzyme shows a dynamical reaction mechanism. In the catalytic site, a water molecule is trapped by the catalytic Tyr155 and Ser142 residues in the vicinity of the bound NAD+ and acetate, substrate binding structure, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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SYSTEMATIC NAME
IUBMB Comments
(R)-3-hydroxybutanoate:NAD+ oxidoreductase
Also oxidizes other 3-hydroxymonocarboxylic acids.
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CAS REGISTRY NUMBER
COMMENTARY
9028-38-0
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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)-2-hydroxybutanoate + NAD+
acetoacetate + NADH
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isoenzyme from heavy mitochondria and isoenzyme from light mitochondria show no significant difference in activity
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?
(R)-3-hydroxybutanoate + 3-acetylpyridine adenine dinucleotide
acetoacetate + 3-acetylpyridine adenine dinucleotideH2
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r
(R)-3-hydroxybutanoate + NADP+
acetoacetate + NADPH
activity with NADP+ is 2% of the activity with NAD+
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?
2-methyl-3-hydroxybutyrate + NAD+
2-methylacetoacetate + NADH
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-
r
4-hydroxybutanoate + NAD+
acetoacetate + NADH
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isoenzyme from heavy mitochondria shows 40% lower activity than enzyme fromlight mitochondria
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?
acetoacetate + NADH + H+
(R)-3-hydroxybutanoate + NAD+
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?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
model of the binding mode of the substrate D-3-hydroxybutyrate, Gln193 is the only residue of the substrate-binding loop that interacts directly with the substrate, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form, overview
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r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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r
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
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the enzyme is involved in poly(3-hydroxybutyrate) biosynthesis together with acetoacetyl-CoA thiolase and PHB synthase, pathway overview, intracellular concentrations of key metabolites, i.e. CoA, acetyl-CoA, 3HB-CoA, NAD+/NADH, determine whether a cell accumulates or degrades PHB
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r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB
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r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
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during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel
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r
3-hydroxyvalerate + NAD+
3-oxovalerate + NADH + H+
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?
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
the reversible reactions occur by shuttle movements of a hydrogen negative ion from the C3 atom of the substrate to the C4 atom of NAD+ and from the C4 atom of NADH to the C3 atom of the product. The reaction may be further coupled to the withdrawal of a proton from the hydroxyl group of the substrate by the ionized Tyr155 residue
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r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH1 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
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r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH2 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
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r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH3 is specialized to utilize 3-hydroxybutyrate
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r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH3 is specialized to utilize 3-hydroxybutyrate
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r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH2 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
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r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH1 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
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r
levulinic acid + NADH + H+
4-hydroxyvaleric acid + NAD+
only the recombinant wild type enzyme with N-terminal His-tag shows activity with levulinic acid
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?
levulinic acid + NADH + H+
4-hydroxyvaleric acid + NAD+
the wild type enzyme shows low activity with levulinic acid, while it's a good substrate for mutant enzyme H144L/W187F
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?
poly-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
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r
poly-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
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r
additional information
?
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no activity of the wild-type enzyme with levulinic acid, enzyme mutant H144L/W187F is active with levulinic acid producing 4-hydroxyvaleric acid
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?
additional information
?
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enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state
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?
additional information
?
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a ketone body converting enzyme in mitochondria in liver jerboa, enzyme expression, activity and metabolism at different physiological states, overview
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?
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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
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
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the enzyme is involved in poly(3-hydroxybutyrate) biosynthesis together with acetoacetyl-CoA thiolase and PHB synthase, pathway overview, intracellular concentrations of key metabolites, i.e. CoA, acetyl-CoA, 3HB-CoA, NAD+/NADH, determine whether a cell accumulates or degrades PHB
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r
acetoacetate + NADH + H+
(R)-3-hydroxybutanoate + NAD+
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?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
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?
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB
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r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
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during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel
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r
additional information
?
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enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state
-
-
?
additional information
?
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-
a ketone body converting enzyme in mitochondria in liver jerboa, enzyme expression, activity and metabolism at different physiological states, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE