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Information on EC 1.1.1.36 - acetoacetyl-CoA reductase
for references in articles please use BRENDA:EC1.1.1.36
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.36 acetoacetyl-CoA reductase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.1.1.36
- polyhydroxyalkanoate
- beta-ketothiolase
- eutropha
-
ralstonia
-
poly3-hydroxybutyrate
- cupriavidus
- necator
-
medium-chain-length
-
2-enoyl-coa
- 3-hydroxyhexanoate
-
enoyl
-
poly3-hydroxybutyrate-co-3-hydroxyhexanoate
-
short-chain-length
- ramigera
- 3-hydroxyalkanoate
-
3r-hydroxyacyl-coas
- trans-2-enoyl-coa
-
phbhhx
-
pha-negative
-
zoogloea
-
r-3-hydroxybutyrate
-
copolyesters
- 3-hydroxyvalerate
-
poly3-hydroxybutyrate-co-3-hydroxyvalerate
- 3-ketothiolase
- scp-2
- synthesis
- biotechnology
showSynonyms
acetoacetyl-coa reductase, mfe-2, akr1b15, nadph-dependent acetoacetyl-coa reductase, ketoacyl reductase, d-3-hydroxyacyl-coa dehydrogenase, (3r)-hydroxyacyl-coa dehydrogenase, acetoacetyl coa reductase, nadh-preferring acetoacetyl-coa reductase, nadph-linked acetoacetyl-coa reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(3R)-hydroxyacyl-CoA dehydrogenase
(R)-3-hydroxyacyl-CoA dehydrogenase
-
-
-
-
AAR
AcAc-CoA reductase
acetoacetyl CoA reductase
acetoacetyl coenzyme A reductase
-
-
-
-
acetoacetyl-CoA reductase
beta-ketoacyl reductase
beta-ketoacyl-CoA reductase
-
-
-
-
D(-)-beta-hydroxybutyryl CoA-NADP oxidoreductase
-
-
-
-
D-3-hydroxyacyl-CoA dehydrogenase
D-3-hydroxyacyl-CoA reductase
-
-
-
-
hydroxyacyl coenzyme-A dehydrogenase
-
-
-
-
MFE-2
MSMEG_6753
NADH-preferring acetoacetyl-CoA reductase
NADP-linked acetoacetyl CoA reductase
-
-
-
-
NADPH-dependent acetoacetyl coenzyme A reductase
NADPH-dependent acetoacetyl-CoA reductase
NADPH-dependent acetoacetyl-coenzyme A reductase
NADPH:acetoacetyl-CoA reductase
-
-
-
-
PHA-specific acetoacetyl-CoA reductase
PhaB
PhbB
polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase
short chain beta-ketoacetyl(acetoacetyl)-CoA reductase
-
-
-
-
additional information
(3R)-hydroxyacyl-CoA dehydrogenase
-
domain of multifunctional enzyme type 2 (MFE-2), (3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
(3R)-hydroxyacyl-CoA dehydrogenase
-
domain of multifunctional enzyme type 2 (MFE-2), (3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
(3R)-hydroxyacyl-CoA dehydrogenase
-
domain of multifunctional enzyme type 2 (MFE-2), (3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
D-3-hydroxyacyl-CoA dehydrogenase
-
part of the multifunctional protein (MFP) containing crotonase, L-3-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and 3-hydroxyacyl-CoA epimerase
D-3-hydroxyacyl-CoA dehydrogenase
-
part of the multifunctional protein (MFP) containing crotonase, L-3-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and 3-hydroxyacyl-CoA epimerase
-
NADH-preferring acetoacetyl-CoA reductase
-
NADPH-dependent acetoacetyl coenzyme A reductase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
NADPH-dependent acetoacetyl-CoA reductase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase
-
-
additional information
FabG belongs to the short-chain dehydrogenase/reductase superfamily, whose members are homologous in sequence and have several conserved motifs
additional information
FabG belongs to the short-chain dehydrogenase/reductase superfamily, whose members are homologous in sequence and have several conserved motifs
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
-
-
-
-
(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
catalytic site structure and catalytic triad Ser151, Tyr164, and Lys168
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered), 4-oxopentanoate degradation, acetyl-CoA fermentation to butanoate, ethylmalonyl-CoA pathway, polyhydroxybutanoate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-41-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxydecanoyl-CoA + NADP+
3-oxodecanoyl-CoA + NADPH + H+
-
Substrates: (3R)-hydroxyacyl-CoA dehydrogenase
Products: -
Products: -
?
(3R)-hydroxybutyryl-CoA + NAD+
3-oxobutylryl-CoA + NADH
-
Substrates: -
Products: -
Products: -
?
(3R)-hydroxybutyryl-CoA + NADP+
3-oxobutyryl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(3R)-hydroxydecanoyl-CoA + NAD+
3-oxodecanoyl-CoA + NADH
-
Substrates: -
Products: -
Products: -
?
(3R)-hydroxyhexadecanoyl-CoA + NADP+
3-oxohexadecanoyl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(R)-3-hydroxybutyryl-CoA
trans-2-butenoyl-CoA + H2O
-
Substrates: dehydration, multifunctional type 2 enzyme
Products: -
Products: -
?
(R)-3-hydroxybutyryl-CoA + NAD+
3-oxobutyryl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
Substrates: oxidation, multifunctional type 2 enzyme
Products: -
Products: -
?
(R)-3-hydroxybutyryl-CoA + NADPH + H+
3-oxobutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxydecanoyl-CoA + NAD+
3-oxodecanoyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
2-methylacetoacetyl-CoA + NADPH
2-methyl-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
? + NADPH
(R)-3-hydroxybutyrylphosphopantetheine + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
D-3-hydroxybutyryl-CoA + NAD+
-
Substrates: PHA-synthesis
Products: -
Products: -
ir
acetoacetyl-CoA + NADH + H+
D-beta-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH
?
-
Substrates: biosynthesis of poly(D-3-hydroxybutyrate)
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutanoyl-CoA +NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
acetoacetyl-pantetheine + NADPH + H+
D-3-hydroxybutyryl-pantetheine + NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-S-(D-pantetheine)11-pivalate + NADPH
3-hydroxybutyryl-S-(D-pantetheine)11-pivalate + NADP+
-
Substrates: -
Products: -
Products: -
?
butyrylacetyl-CoA + NADPH
3-hydroxyhexanoyl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
D-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
-
Substrates: -
Products: -
Products: -
r
propionylacetyl-CoA + NADPH
3-hydroxypentanoyl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Substrates: -
Products: -
Products: -
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: low activity
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
L-beta-hydroxybutyryl-CoA + NAD+
-
Substrates: reverse only with L-form
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
L-beta-hydroxybutyryl-CoA + NAD+
Methylorubrum rhodesianum MB 126
-
Substrates: reverse only with L-form
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
ir
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
Pigeon
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
Pigeon
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
ir
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: step in the biosynthesis of polyhydroxybutyrate, a biodegradable thermoplastic polymer
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: step in the enzyme-catalyzed synthesis system for production of poly(3-hydroxybutyrate) in vitro, overview
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: high activity
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
Substrates: reverse only with D-form
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
Methylorubrum rhodesianum MB 126
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
Methylorubrum rhodesianum MB 126
-
Substrates: reverse only with D-form
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
Pigeon
-
Substrates: -
Products: -
Products: -
ir
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
Substrates: -
Products: -
Products: -
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
Substrates: -
Products: -
Products: -
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
Substrates: -
Products: -
Products: -
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
Pigeon
-
Substrates: -
Products: -
Products: -
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
Substrates: -
Products: -
Products: -
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
Substrates: -
Products: -
Products: -
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: KCR catalyzes the first reduction during elongation of very-long-chain fatty acids, VLCFA, precursors of sphingolipids, triacylglycerols, cuticular waxes, and suberin in plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: the N-terminal enzyme part harbors 2 different (3R)-hydroxyacyl-CoA dehydrogenase activities with different substrate specificities, while the 2-enoyl-CoA hydratase 2 activity is located in the C-terminus
Products: -
Products: -
?
additional information
?
-
Substrates: no oxidation of (R/S)-3-hydroxybutyryl-CoA is detected when using NADP+ as cofactor
Products: -
Products: -
?
additional information
?
-
Substrates: no oxidation of (R/S)-3-hydroxybutyryl-CoA is detected when using NADP+ as cofactor
Products: -
Products: -
?
additional information
?
-
Substrates: no activity is detected when NADPH is replaced by NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity is detected when NADPH is replaced by NADH
Products: -
Products: -
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
Substrates: no activity is detected when NADPH is replaced by NADH
Products: -
Products: -
?
additional information
?
-
Substrates: no activity is detected when NADPH is replaced by NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: a point mutation in the dehydrogenase region of the enzyme causes peroxisomal disease leading to severe abnormalities and an early death
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: crotonyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: poor substrate: D-3-hydroxyvaleryl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: L-3-hydroxyacyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: D-3-hydroxyacyl-CoA's with chain length exceeding 6
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxybutyryl-CoA
trans-2-butenoyl-CoA + H2O
-
Substrates: dehydration, multifunctional type 2 enzyme
Products: -
Products: -
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
Substrates: oxidation, multifunctional type 2 enzyme
Products: -
Products: -
?
(R)-3-hydroxybutyryl-CoA + NADPH + H+
3-oxobutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
D-3-hydroxybutyryl-CoA + NAD+
-
Substrates: PHA-synthesis
Products: -
Products: -
ir
acetoacetyl-CoA + NADPH
?
-
Substrates: biosynthesis of poly(D-3-hydroxybutyrate)
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Substrates: -
Products: -
Products: -
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
Substrates: low activity
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
Substrates: step in the biosynthesis of polyhydroxybutyrate, a biodegradable thermoplastic polymer
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: high activity
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
Substrates: PHB synthesis
Products: -
Products: -
?
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: KCR catalyzes the first reduction during elongation of very-long-chain fatty acids, VLCFA, precursors of sphingolipids, triacylglycerols, cuticular waxes, and suberin in plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: a point mutation in the dehydrogenase region of the enzyme causes peroxisomal disease leading to severe abnormalities and an early death
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
binding mode and conformation of NAD+ bound to the enzyme derived from the crystal structure, overview
NADPH
-
B-specific, i.e. transfer of pro-S-hydrogen from NADPH to acetoacetyl-CoA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetoacetyl-CoA
-
NADH-linked, less sensitive; NADPH-linked, concentration above 0.025 mM, nearly independent of NADPH concentrations 0.03-0.5 mM
acetoacetyl-CoA
-
markedly at concentrations above 0.005 mM and NADPH 0.01 mM, less inhibition when NADPH increases from 0.01 to 1 mM
additional information
-
NADH-linked: not inhibited by NADPH at concentrations of 1 mM, NADPH-linked: not inhibited by NAD+ at concentrations of 1 mM
-
additional information
Pigeon
-
not inhibited by p-hydroxymercuribenzoate or N-ethylmaleimide from 0.1-10 mM
-
additional information
-
not inhibited by acetoacetyl-CoA at high concentrations
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
acetoacetyl-coa reductase deficiency
The role of alpha-methylacyl-CoA racemase in bile acid synthesis.
acetoacetyl-coa reductase deficiency
Yeast peroxisomal multifunctional enzyme: (3R)-hydroxyacyl-CoA dehydrogenase domains A and B are required for optimal growth on oleic acid.
alpha-methylacyl-coa racemase deficiency
Clinical consequences of defects in peroxisomal beta-oxidation.
Neoplasms
Engineering aldo-keto reductase 1B10 to mimic the distinct 1B15 topology and specificity towards inhibitors and substrates, including retinoids and steroids.
Neoplasms
Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase.
Tuberculosis
Selection of an Escherichia coli host that expresses mutant forms of Mycobacterium tuberculosis 2-trans enoyl-ACP(CoA) reductase and 3-ketoacyl-ACP(CoA) reductase enzymes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0567
acetoacetyl-CoA
recombinant enzyme, with NADH as cosubstrate, at pH 7.5 and 25°C
0.318
acetoacetyl-CoA
recombinant enzyme, with NADPH as cosubstrate, at pH 7.5 and 25°C
0.0077
NADH
recombinant enzyme, at pH 7.5 and 25°C
0.0443
NADPH
recombinant enzyme, at pH 7.5 and 25°C
additional information
additional information
Michaelis-Menten kinetics, binding of dinucleotide cofactors to AKR1B15.1, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, binding of dinucleotide cofactors to AKR1B15.1, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.095
NADPH
recombinant enzyme, at pH 7.5 and 25°C
0.131
acetoacetyl-CoA
recombinant enzyme, with NADPH as cosubstrate, at pH 7.5 and 25°C
11.6
acetoacetyl-CoA
recombinant enzyme, with NADH as cosubstrate, at pH 7.5 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.023
0.07
native enzyme, forward reaction, using NADPH as cosubstrate, at pH 7.5 and 25°C
0.25
recombinant enzyme, forward reaction, using NADPH as cosubstrate, at pH 7.5 and 25°C
0.43
-
(R)-3-hydroxybutyryl-CoA as substrate, activity of D-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-II
0.53 - 0.62
-
recombinant enzyme in transformed Escherichia coli strain DH5alpha
0.58
-
(R)-3-hydroxydecanoyl-CoA as substrate, activity of D-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-II
0.61
native enzyme, backward reaction, using NADH as cosubstrate, at pH 7.5 and 25°C
1.23
-
enzyme from recombinant strain, monitored at 340 nm by the depletion of NADPH during the reaction.
1.96
recombinant enzyme, forward reaction, using NADH as cosubstrate, at pH 7.5 and 25°C
125
-
last purification step, 5.9fold purification. Candida tropicalis recombinant (3R)-hydroxyacyl-CoA dehydrogenase [CiMFE-2(h2delta)] from Escherichia coli
14
native enzyme, forward reaction, using NADH as cosubstrate, at pH 7.5 and 25°C
additional information
additional information
-
fatty acid and cuticular wax composition in wild-type and mutant plants, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pigeon
alignment of nucleotide-binding site from human MFE-2 with Saccharomyces cerevisiae and Candida tropicalis MFE-2 shown
-
-
brenda
alignment of nucleotide-binding site from human MFE-2 with Saccharomyces cerevisiae and Candida tropicalis MFE-2 shown
-
-
brenda
alignment of the amino acid sequence of the hydratase 2 domain from human MFE-2 with those of other known hydratase 2 domains from eukaryotes shown
-
-
brenda
alignment of nucleotide-binding site from human MFE-2 with Saccharomyces cerevisiae and Candida tropicalis MFE-2 shown
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isozyme AKR1B15.1, very low expression of isozyme AKR1B15.2
brenda
additional information
additional information
isozyme tissue-specific expression analysis, overview
brenda
additional information
-
isozyme tissue-specific expression analysis, overview
brenda
additional information
-
addition of acetate (0.1-10 mM) to culture medium of rice seedlings does not increase the content of poly-3-hydroxybutyrate in the rice root or leaf. Enzyme activity is not clearly detectable in rice seedlings
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme contains a C-terminal peroxisomal targeting signal sequence
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
-
KCR catalyzes the first reduction during elongation of very-long-chain fatty acids, VLCFA, precursors of sphingolipids, triacylglycerols, cuticular waxes, and suberin in plants, but only AtKCR1 is a functional KCR isoform involved in microsomal fatty acid elongation
metabolism
the enzyme is rate-limiting in poly(3-hydroxybutyrate) biosynthesis. Poly(3-hydroxybutyrate) (P(3HB)) is synthesized from acetyl-CoA via three successive reactions. Two molecules of acetyl-CoA are condensed into acetoacetyl-CoA by a beta-ketothiolase (PhaA). Then NADPH-dependent acetoacetyl-CoA reductase (PhaB) converts acetoacetyl-CoA into (R)-3-hydroxybutyryl-CoA (3HB-CoA), which is finally polymerized into P(3HB) by polyhydroxyalkanoate synthase (PhaC)
metabolism
-
poly-3-hydroxybutyrate (PHB) is generated from from acetyl CoA by the consecutive reaction of three enzymes: beta-ketothiolase (EC 2.3.1.9), acetoacetyl CoA reductase (EC 1.1.1.36) and PHB synthase (EC 2.3.1.) in rice roots
metabolism
-
poly-3-hydroxybutyrate (PHB) is generated from from acetyl CoA by the consecutive reaction of three enzymes: beta-ketothiolase (EC 2.3.1.9), acetoacetyl CoA reductase (EC 1.1.1.36) and PHB synthase (EC 2.3.1.) in corn roots
metabolism
-
poly-3-hydroxybutyrate (PHB) is generated from from acetyl CoA by the consecutivereaction of three enzymes: beta-ketothiolase (EC 2.3.1.9), acetoacetyl CoA reductase (EC 1.1.1.36) and PHB synthase (EC 2.3.1.) in rice roots
metabolism
AKR1B15.1 is a mitochondrial carbonyl reductase. Two alternatively spliced protein isoforms encoded by the human AKRgene AKR1B15 exist, the AKR1B15.1 isoform catalyzes reduction of steroids and 3-keto-acyl-CoA conjugates
metabolism
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the enzyme is rate-limiting in poly(3-hydroxybutyrate) biosynthesis. Poly(3-hydroxybutyrate) (P(3HB)) is synthesized from acetyl-CoA via three successive reactions. Two molecules of acetyl-CoA are condensed into acetoacetyl-CoA by a beta-ketothiolase (PhaA). Then NADPH-dependent acetoacetyl-CoA reductase (PhaB) converts acetoacetyl-CoA into (R)-3-hydroxybutyryl-CoA (3HB-CoA), which is finally polymerized into P(3HB) by polyhydroxyalkanoate synthase (PhaC)
-
physiological function
-
suppressed KCR activity results in a reduction of cuticular wax load and affects VLCFA composition of sphingolipids, seed triacylglycerols, and root glycerolipids
physiological function
the enzyme is dispensable for mycobacterial growth
physiological function
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
the enzyme is dispensable for mycobacterial growth
-
physiological function
-
the enzyme is dispensable for mycobacterial growth
-
additional information
PhaB forms a ternary complex with NADPH and acetoacetyl-CoA
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
PhaB forms a ternary complex with NADPH and acetoacetyl-CoA
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PHAB_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
246
0
26370
Swiss-Prot
-
PHAB_ALLVD
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
246
0
26124
Swiss-Prot
other Location (Reliability: 3)
PHAB_ACISR
248
0
26727
Swiss-Prot
other Location (Reliability: 4)
PHAB_SYNY3
Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
240
0
25333
Swiss-Prot
-
A0R723_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
240
0
24569
TrEMBL
other Location (Reliability: 3)
C7RM91_ACCRE
Accumulibacter regalis
247
0
25926
TrEMBL
other Location (Reliability: 1)
G0HY85_HALHT
Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)
312
0
32919
TrEMBL
-
Q4UN54_RICFE
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
241
0
26252
TrEMBL
-
B4EAU4_BURCJ
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
247
0
26383
TrEMBL
Secretory Pathway (Reliability: 1)
Q3JRS9_BURP1
Burkholderia pseudomallei (strain 1710b)
248
0
26738
TrEMBL
-
Q3JJT1_BURP1
Burkholderia pseudomallei (strain 1710b)
248
0
26457
TrEMBL
-
Q8NMW9_CORGL
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
236
0
25288
TrEMBL
-
FABV_TREDE
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)
397
0
43759
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
250000
42000
-
NADH-linked enzyme: x * 55000, NADPH-linked enzyme: x * 42000, SDS-PAGE
92000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
crystal structure, enzyme shows a alpha/beta short chain alcohol dehydrogenase/reductase, i.e. SDR, fold
heterodimer
-
residues 1-313 and 314-604 forming the dehydrogenase A and B units, respectively
homotetramer
tetramer
additional information
-
the recombinant truncated and selenomethionine-labeled enzyme has a molecular weight of 34602 Da as determined by mass spectrometry
?
-
NADH-linked enzyme: x * 55000, NADPH-linked enzyme: x * 42000, SDS-PAGE
?
Methylorubrum rhodesianum MB 126
-
NADH-linked enzyme: x * 55000, NADPH-linked enzyme: x * 42000, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5 mg/ml purified recombinant, detagged truncated enzyme, amino acid residues 1-604, by vapor diffusion technique, 20°C, in 30% PEG 4000, 0.1 M sodium acetate, pH 4.2, 0.2 M ammonium acetate, equal volume of 0.002 ml of protein and precipitant solution, 11% v/v glycerol as cryoprotectant, X-ray diffraction structure determination and analysis at 2.22-2.36 A resolution, the wild-type enzyme, comprising amino acid residues 1-906, is unstable and not crystallizable
-
purified recombinant His-tagged wild-type and mutant enzymes in complex with NADP+ and acetoacetyl-CoA, wild-type protein crystals grow from 0.1 M MES, pH 7.1, 0.9 mM NADP+, 0.9 mM acetoacetyl-CoA, 1.6 M ammonium sulfate, and 10% 1,4-dioxane, mutant crystals grow from 0.6-1.2 M sodium-potassium tartrate, 0.16-0.20 M lithium sulfate, and 0.1 M CHES, pH 8.9-9.9, X-ray diffraction structure determination and analysis at 1.8 A and 2.0-2.9 A resolution, respectively, molecular replacement method using the structure of FabG from Escherichia coli, PDB ID 1I01, as the search probe
apo and NADP+-bound enzyme forms, sitting drop vapor diffusion method, using 100 mM Na-HEPES (pH 7.5), 30% (v/v) PEG 400 and 200 mM magnesium chloride hexahydrate for the apo enzyme and 200 mM sodium citrate tribasic dehydrate and 20% (w/v) PEG 3350 for the NADP+-bound enzyme
selenomethionine-labeled recombinant truncated enzyme, X-ray diffraction structure determination and analysis at 2.38 A resolution
-
sitting drop vapor diffusion method, using 10% (w/v) PEG 8000, 8% (w/v) ethylene glycol, 100 mM HEPES-NaOH pH 7.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q47L
T173S
Q47L
-
the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
-
T173S
-
the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
-
Q47L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
random mutagenesis, the mutant exhibits a kcat value 2.4fold higher compared to the wild-type enzyme, enhanced activity, and enhanced P(3HB) accumulation when expressed in recombinant Corynebacterium glutamicum. The mutation affects the interaction with substrates, resulting in the acquirement of enhanced activity
-
T173S
E366A
-
site-directed mutagenesis, kcat/Km 100times lower than that of the wild type
truncated version
additional information
Q47L
random mutagenesis, the mutant exhibits a kcat value 2.4fold higher compared to the wild-type enzyme, enhanced activity, and enhanced P(3HB) accumulation when expressed in recombinant Corynebacterium glutamicum. The mutation affects the interaction with substrates, resulting in the acquirement of enhanced activity
Q47L
the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
T173S
random mutagenesis, the mutant exhibits a kcat value 3.5fold higher compared to the wild-type enzyme, enhanced activity, and enhanced P(3HB) accumulation when expressed in recombinant Corynebacterium glutamicum. The mutation affects the interaction with substrates, resulting in the acquirement of enhanced activity
T173S
by random mutagenesis and high-throughput screening, enzyme mutant engineering for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system
T173S
the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
T173S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
random mutagenesis, the mutant exhibits a kcat value 3.5fold higher compared to the wild-type enzyme, enhanced activity, and enhanced P(3HB) accumulation when expressed in recombinant Corynebacterium glutamicum. The mutation affects the interaction with substrates, resulting in the acquirement of enhanced activity
-
T173S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
by random mutagenesis and high-throughput screening, enzyme mutant engineering for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system
-
truncated version
-
truncated version (lacking the carboxyl-terminal 271 amino acids). The truncated form contains only the D-3-hydroxyacyl-CoA dehydrogenase activity
truncated version
-
truncated version (lacking the carboxyl-terminal 271 amino acids). The truncated form contains only the D-3-hydroxyacyl-CoA dehydrogenase activity
-
additional information
-
loss of AtKCR1 function results in embryo lethality, which cannot be rescued by AtKCR2 expression using the AtKCR1 promoter. Disruption of the AtKCR2 gene has no obvious phenotypic effect. Suppressed KCR activity results in a reduction of cuticular wax load and affects VLCFA composition of sphingolipids, seed triacylglycerols, and root glycerolipids, phenotypes, detailed overview
additional information
-
site-directed mutagenesis, while the wild-type enzyme, comprising amino acid residues 1-906, is unstable and not crystallizable, as is the recombinant truncated version comprising amino acid residues 1-591, the mutants 1-604 and 1-612, with or without further modifications, are stable with different crystallizability, overview
additional information
-
the Candida tropicalis MFE-2 with a deleted hydratase 2 domain (Ct MFE-2(h2delta)) and mutational variants of the A and B domains (Ct MFE-2(h2deltaadelta), Ct MFE-2(h2deltabdelta), and Ct MFE-2(h2deltaadeltabdelta)) are overexpressed and characterized
additional information
-
construction of transgenic Zea mays plants, by microprojectile bombardment, expression of the enzyme from Alcaligenes eutrophus using the small subunit 24 amino acid transit peptide of Pisum sativum ribulose bisphosphate carboxylase to target the plasmid into the chloroplasts of maize
additional information
directed evolution and structural analysis of NADPH-dependent acetoacetyl-CoA reductase reveals two mutations responsible for enhanced kinetics, enzyme mutant is engineered by means of directed evolution consisting of an error-prone PCR-mediated mutagenesis and a P(3HB) accumulation-based in vivo screening system using Escherichia coli. Comparative three-dimensional structural analysis of wild-type PhaB and highly active PhaB mutants reveals that the beneficial mutations affect the flexibility around the active site, which in turn play an important role in substrate recognition. Both the kinetic analysis and crystal structure data support the conclusion that PhaB forms a ternary complex with NADPH and acetoacetyl-CoA
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
directed evolution and structural analysis of NADPH-dependent acetoacetyl-CoA reductase reveals two mutations responsible for enhanced kinetics, enzyme mutant is engineered by means of directed evolution consisting of an error-prone PCR-mediated mutagenesis and a P(3HB) accumulation-based in vivo screening system using Escherichia coli. Comparative three-dimensional structural analysis of wild-type PhaB and highly active PhaB mutants reveals that the beneficial mutations affect the flexibility around the active site, which in turn play an important role in substrate recognition. Both the kinetic analysis and crystal structure data support the conclusion that PhaB forms a ternary complex with NADPH and acetoacetyl-CoA
-
additional information
disruption or knockout of fabG1 abolishes HA synthesis, and complementation of the DELTAfabG1 mutant with the fabG1 gene restores both PHA synthesis capability and the NADPH-dependent acetoacetyl-CoA reductase activity. Heterologous coexpression of the PHA synthase genes, phaEC together with fabG1, but not its five paralogs, reconstructs the PHA biosynthetic pathway in Haloferax volcanii, a PHA-defective haloarchaeon
additional information
-
disruption or knockout of fabG1 abolishes HA synthesis, and complementation of the DELTAfabG1 mutant with the fabG1 gene restores both PHA synthesis capability and the NADPH-dependent acetoacetyl-CoA reductase activity. Heterologous coexpression of the PHA synthase genes, phaEC together with fabG1, but not its five paralogs, reconstructs the PHA biosynthetic pathway in Haloferax volcanii, a PHA-defective haloarchaeon
additional information
-
disruption or knockout of fabG1 abolishes HA synthesis, and complementation of the DELTAfabG1 mutant with the fabG1 gene restores both PHA synthesis capability and the NADPH-dependent acetoacetyl-CoA reductase activity. Heterologous coexpression of the PHA synthase genes, phaEC together with fabG1, but not its five paralogs, reconstructs the PHA biosynthetic pathway in Haloferax volcanii, a PHA-defective haloarchaeon
-
additional information
-
constructs are tested for complementation in Saccharomyces cerevisiae
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris/HCl buffer, pH 7.5, 10 mM 2-mercaptoethanol, 50% glycerol, several months
-
0°C and -20°C, 10 mM Tris/HCl buffer, pH 7.5, 10 mM 2-mercaptoethanol, rather unstable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, DEAE-Sephasrose CL-6B, hydroxyapatite, Red-Sepharose CL-6B chromatography
-
ammonium sulfate fractionation, hydroxylapatite, Sephadex G-200 chromatography
-
ammonium sulfate fractionation, ion exchange, hydroxyapatite, affinity chromatography
-
Candida tropicalis recombinant (3R)-hydroxyacyl-CoA dehydrogenase [CiMFE-2(h2delta)] from Escherichia coli
-
gel-filtration Sephadex G-200, DEAE-cellulose chromatography, sucrose-gradient centrifugation
-
HisTrap column chromatography
NADH-linked: DEAE-Sepharose CL-6B, Blue Sepharose CL-6B, botyl Sepharose 4B, Mono Q 5/5
-
NADPH-linked: DEAE-Sepharose CL-6B, Red 120-agarose, phenyle Sepharose
-
recombinant His-tagged enzyme from Escherichia coli by nickel-affinity chromatography
-
recombinant His-tagged isozymes AKR1B15.1 and AKR1B15.2 isozymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged, truncated enzyme from Escherichia coli, the His-tag is cleaved off by factor Xa
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Resource S cation exchange chromatography and Superdex 200 HR 10/30 column chromatography
-
the FOX2 gene is overexpressed from a multicopy vector (YEp352) in Saccharomyces cerevisiae and the gene product purified to apparent homogenity. A truncated version of MFP lacking 271 carboxyl-terminal amino acids is also overexpressed and purified
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the yeast expression plasmid pYE352, Saccharomyces cerevisiae fox-2 cells, devoid of Sc MFE-2, transformed with pYE352::ScMFE-2(adelta) and pYE352::ScMFE-2(bdelta). The recombinant (3R)-hydroxyacyl-CoA dehydrogenase [CiMFE-2(h2delta)] transformed into Escherichia coli
-
DNA sequence determination and analysis, construction of 5 different expression constructs for transformation of Zea mays plants, one of which contains the small subunit 24 amino acid transit peptide of Pisum sativum ribulose bisphosphate carboxylase
-
expressed in Brassica napus, transported with fusion peptide to seed leukoplast
-
expressed in Escherichia coli BL21 Rosetta2 (DE3) pLysS cells and a fabG -temperature-sensitive mutant Escherichia coli CL104 strain
expressed in Escherichia coli BL21(DE3) cells
expression of a truncated enzyme, comprising residues Met1-Asp319 of the dehydrogenase region, lacking the hydratase-2 region, in Escherichia coli
-
functional co-expression of PHA synthesis genes phaAB in Aeromonas hydrophila 4AK4 encoding beta-ketothiolase and the NADPH-dependent acetoacetyl-CoA reductase, leading to production of terpolyester poly(3-hydroxybutyrate-co-3-hydroxyvalerate-co-3-hydroxyhexanoate), addition of propionate alters the monomer composition of the polymer, overview
-
gene AKR1B15 located on chromosome 7, cloning of two isoforms: AKR1B15.1 and AKR1B15.2, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged isozymes in Escherichia coli strain BL21(DE3), recombinant expression of C- or N-terminally c-Myctagged isozymes in HEK-293 cells
gene fabG1, DNA sequence determination and analysis, expression in the fabG1-deficient mutant, phylogenetic tree, sequence comparison of FabG1 to FabG6
gene phaB, expression of the N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene phaB, recombinant expression in Corynebacterium glutamicum strain ATCC 13803, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene phaB, recombinant expression of a PhaB mutant T173s enzyme from Ralstonia eutropha in Nicotiana tabacum cv. Bright Yellow-2 cells, the mutated PhaB increases the poly(3-hydroxybutyrate) (P(3HB)) content by threefold compared to control. Plasmids pRIphaC-phaB(WT) and pRIphaCphaB(TS) are introduced into BY-2 cells using the Agrobacterium-mediated transfection method. The PhaB-catalyzed reaction is suggested to be a rate-limiting step of P(3HB) biosynthesis in tobacco BY-2 cells
gene phbB, functional expression in Escherichia coli strains BW25113 and DH5alpha, co-expression with genes phbA and tesB, encoding beta-ketothiolase and thioesterase II, respectively, to reconstruct the R-3-hydroxybutyric acid production pathway, optimization of culture conditions, overview
-
gene phbB, functional expression of the phaABCRe operon containing genes phbA, phbB and phbC of the PHA biosynthetic pathway of Ralstonia eutropha, which encode beta-ketothiolase, NADPH-linked acetoacetyl-CoA reductase and PHA synthase, respectively, in Saccharomyces cerevisiae strain INVSc1/PHA1 and in non-convenient Kloeckera spp. strain KY1/PHA, reconstruction of the PHA biosynthetic pathway leading to accumulation of poly-3-hydroxybutyrate and copolymer poly-(3-hydroxybutyrate-co-poly-3-hydroxyvalerate), respectively, overview
-
isozymes KCR1 and KCR2, DNA and amino acid sequence determination, expression analysis, complementation of the yeast ybr159D mutant only isozyme KCR1, overview
-
N-terminal part of amino acids 1-604 is expressed as a C-terminally His-tagged, stable protein in Escherichia coli strain BL21(DE3)
-
wild type (HsMFE-2) and its variants are expressed in Saccharomyces cerevisiae
-
expressed in Escherichia coli BL21(DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
construction an evaluation of a polyhydroxybutyrate production system using Zea mays chloroplasts expressing the enzyme from Alcaligenes eutrophus
synthesis
synthesis
-
establishing of an enzyme-catalyzed synthesis system for production of poly(3-hydroxybutyrate) in vitro on the basis of the poly(3-hydroxybutyrate) biosynthesis pathway of Ralstonia eutropha, recycling CoA for synthesis of acetyl-CoA and deriving NADPH from regeneration by GDH, overview
synthesis
the engineered enzyme mutant T173S can be used for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system
synthesis
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the engineered enzyme mutant T173S can be used for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system
-
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REF.
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JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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brenda
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256
6282-6290
1981
Anser sp., Bos taurus, Gallus gallus, Pigeon, Rattus norvegicus, Saccharomyces cerevisiae
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11
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1973
Streptomyces coelicolor
-
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Prasad, M.R.; Cook, L.; Vieth, R.; Cinti, D.L.
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Rattus norvegicus
brenda
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246
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1986
Rattus norvegicus
brenda
Fukui, T.; Ito, M.; Saito, T.; Tomita, K.
Purification and characterization of NADP-linked acetoacetyl-CoA reductase from Zoogloea ramigera I-16-M
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917
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1987
Pigeon, Zoogloea ramigera
brenda
Ploux, O.; Masamune, S.; Walsh, C.T.
The NADPH-linked acetoacetyl-CoA reductase from Zoogloea ramigera. Characterization and mechanistic studies of the cloned enzyme over-produced in Escherichia coli
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174
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1988
Zoogloea ramigera
brenda
Amos, D.A.; McInerney, M.J.
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159
16-20
1993
Zoogloea ramigera, Azotobacter beijerinckii, Syntrophomonas wolfei, Cupriavidus necator
-
brenda
Belova, L.L.; Sokolov, A.P.; Sidorov, I.A.; Trotsenko, Y.A.
Purification and characterization of NADPH-dependent acetoacetyl-CoA reductase from Methylobacterium extorquens
FEMS Microbiol. Lett.
156
275-279
1997
Zoogloea ramigera, Methylorubrum extorquens, Methylorubrum rhodesianum, Cupriavidus necator, Azotobacter vinelandii, Rhodospirillum rubrum, Methylorubrum extorquens 15, Methylorubrum rhodesianum MB 126
-
brenda
Mothes, G.; Babel, W.
Methylobacterium rhodesianum MB 126 possesses two acetoacetyl-CoA reductases
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161
277-280
1994
Zoogloea ramigera, Methylorubrum rhodesianum, Rhodospirillum rubrum, Rhodococcus ruber, Methylorubrum rhodesianum MB 126
-
brenda
Gerngross, T.U.; Martin, D.P.
Enzyme-catalyzed synthesis of poly[(R)-(-)-3-hydroxybutyrate]: Formation of macroscopic granules in vitro
Proc. Natl. Acad. Sci. USA
92
6279-6283
1995
Cupriavidus necator
brenda
Houmiel, K.L.; Slater, S.; Broyles, D.; Casagrande, L.; Colburn, S.; Gonzalez, K.; Mitsky, T.A.; Reiser, S.E.; Shah, D.; Taylor, N.B.; Tran, M.; Valentin, H.E.; Gruys, K.J.
Poly(beta-hydroxybutyrate) production in oilseed leukoplasts of Brassica napus
Planta
209
547-550
1999
Cupriavidus necator
brenda
Qin, Y.M.; Haapalainen, A.M.; Kilpelainen, S.H.; Marttila, M.S.; Koski, M.K.; Glumoff, T.; Novikov, D.K.; Hiltunen, J.K.
Human peroxisomal multifunctional enzyme type 2: site-directed mutagenesis studies show the importance of two protic residues for 2-enoyl-CoA hydratase 2 activity
J. Biol. Chem.
275
4965-4972
2000
Homo sapiens
brenda
Ylianttila, M.S.; Qin, Y.M.; Hiltunen, J.K.; Glumoff, T.
Site-directed mutagenesis to enable and improve crystallizability of Candida tropicalis (3R)-hydroxyacyl-CoA dehydrogenase
Biochem. Biophys. Res. Commun.
324
25-30
2004
Candida tropicalis
brenda
Satoh, Y.; Tajima, K.; Tannai, H.; Munekata, M.
Enzyme-catalyzed poly(3-hydroxybutyrate) synthesis from acetate with CoA recycling and NADPH regeneration in vitro
J. Biosci. Bioeng.
95
335-341
2003
Cupriavidus necator
brenda
Zhong, H.; Teymouri, F.; Chapman, B.; Maqbool, S.B.; Sabzikar, R.; El-Maghraby, Y.; Dale, B.; Sticklen, M.B.
The pea (Pisum sativum L.) rbcS transit peptide directs the Alcaligenes eutrophus polyhydroxybutyrate enzymes into maize (Zea mays L.) chloroplasts
Plant Sci.
165
455-462
2003
Cupriavidus necator
-
brenda
Haapalainen, A.M.; Koski, M.K.; Qin, Y.M.; Hiltunen, J.K.; Glumoff, T.
Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution
Structure
11
87-97
2003
Rattus norvegicus
brenda
Qiu, Y.Z.; Han, J.; Chen, G.Q.
Metabolic engineering of Aeromonas hydrophila for the enhanced production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate)
Appl. Microbiol. Biotechnol.
69
537-542
2006
Aeromonas hydrophila, Cupriavidus necator
brenda
Zhang, J.; Hao, N.; Chen, G.Q.
Effect of expressing polyhydroxybutyrate synthesis genes (phbCAB) in Streptococcus zooepidemicus on production of lactic acid and hyaluronic acid
Appl. Microbiol. Biotechnol.
71
222-227
2006
Streptococcus equi
brenda
Qiu, Y.Z.; Han, J.; Guo, J.J.; Chen, G.Q.
Production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from gluconate and glucose by recombinant Aeromonas hydrophila and Pseudomonas putida
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27
1381-1386
2005
Aeromonas hydrophila, Aeromonas hydrophila 4AK4, Pseudomonas putida
brenda
Ylianttila, M.S.; Pursiainen, N.V.; Haapalainen, A.M.; Juffer, A.H.; Poirier, Y.; Kalervo Hiltunen, J.; Glumoff, T.
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358
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2006
Candida tropicalis
brenda
Liu, Q.; Ouyang, S.P.; Chung, A.; Wu, Q.; Chen, G.Q.
Microbial production of R-3-hydroxybutyric acid by recombinant E. coli harboring genes of phbA, phbB, and tesB
Appl. Microbiol. Biotechnol.
76
811-818
2007
Cupriavidus necator, no activity in Escherichia coli, no activity in Escherichia coli DH5-alpha
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Biosynthesis of biodegradable polyhydroxyalkanotes biopolymers in genetically modified yeasts
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4
513-520
2007
Cupriavidus necator
-
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Hiltunen, J.K.; Wenzel, B.; Beyer, A.; Erdmann, R.; Fossa, A.; Kunau, W.H.
Peroxisomal multifunctional beta-oxidation protein of Saccharomyces cerevisiae. Molecular analysis of the fox2 gene and gene product
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267
6646-6653
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Saccharomyces cerevisiae, Saccharomyces cerevisiae fox2
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Qin, Y.M.; Marttila, M.S.; Haapalainen, A.M.; Siivari, K.M.; Glumoff, T.; Hiltunen, J.K.
Yeast peroxisomal multifunctional enzyme: (3R)-hydroxyacyl-CoA dehydrogenase domains A and B are required for optimal growth on oleic acid
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274
28619-28625
1999
Candida tropicalis, Homo sapiens, Saccharomyces cerevisiae
brenda
Zhao, W.; Chen, G.
Production and characterization of terpolyester poly(3-hydroxybutyrate-co-3-hydroxyvalerate-co-3-hydroxyhexanoate) by recombinant Aeromonas hydrophila 4AK4 harboring genes phaAB
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42
1342-1347
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Cupriavidus necator
-
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Beaudoin, F.; Wu, X.; Li, F.; Haslam, R.P.; Markham, J.E.; Zheng, H.; Napier, J.A.; Kunst, L.
Functional characterization of the Arabidopsis beta-ketoacyl-coenzyme A reductase candidates of the fatty acid elongase
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150
1174-1191
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Arabidopsis thaliana
brenda
Han, J.; Lu, Q.; Zhou, L.; Liu, H.; Xiang, H.
Identification of the polyhydroxyalkanoate (PHA)-specific acetoacetyl coenzyme A reductase among multiple FabG paralogs in Haloarcula hispanica and reconstruction of the PHA biosynthetic pathway in Haloferax volcanii
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75
6168-6175
2009
Haloarcula hispanica (G0HY85), Haloarcula hispanica, Haloarcula hispanica DSM 4426 (G0HY85)
brenda
Matsumoto, K.; Tanaka, Y.; Watanabe, T.; Motohashi, R.; Ikeda, K.; Tobitani, K.; Yao, M.; Tanaka, I.; Taguchi, S.
Directed evolution and structural analysis of NADPH-dependent acetoacetyl coenzyme A (acetoacetyl-CoA) reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics
Appl. Environ. Microbiol.
79
6134-6139
2013
Cupriavidus necator (P14697), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (P14697)
brenda
Blaise, M.; Van Wyk, N.; Baneres-Roquet, F.; Guerardel, Y.; Kremer, L.
Binding of NADP+ triggers an open-to-closed transition in a mycobacterial FabG beta-ketoacyl-ACP reductase
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474
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Mycolicibacterium smegmatis (A0R723), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2155 (A0R723)
brenda
Yokoo, T.; Matsumoto, K.; Ooba, T.; Morimoto, K.; Taguchi, S.
Enhanced poly(3-hydroxybutyrate) production in transgenic tobacco BY-2 cells using engineered acetoacetyl-CoA reductase
Biosci. Biotechnol. Biochem.
79
986-988
2015
Cupriavidus necator (P14697), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (P14697)
brenda
Weber, S.; Salabei, J.K.; Moeller, G.; Kremmer, E.; Bhatnagar, A.; Adamski, J.; Barski, O.A.
Aldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto reductase with activity toward steroids and 3-keto-acyl-CoA conjugates
J. Biol. Chem.
290
6531-6545
2015
Homo sapiens (C9JRZ8), Homo sapiens
brenda
Tsuda, H.; Shiraki, M.; Inoue, E.; Saito, T.
Generation of poly-beta-hydroxybutyrate from acetate in higher plants: detection of acetoacetyl CoA reductase- and PHB synthase-activities in rice
J. Plant Physiol.
201
9-16
2016
Kalanchoe pinnata, Oryza sativa, Zea mays
brenda
Rodarte, J.V.; Abendroth, J.; Edwards, T.E.; Lorimer, D.D.; Staker, B.L.; Zhang, S.; Myler, P.J.; McLaughlin, K.J.
Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis
Acta Crystallogr. Sect. F
77
54-60
2021
Rickettsia felis (Q4UN54), Rickettsia felis, Rickettsia felis ATCC VR-1525 (Q4UN54)
brenda
Olavarria, K.; Quakkelaar, C.; van Renselaar, J.; Langerak, D.; van Loosdrecht, M.C.M.; Wahl, S.A.
NADH-driven poly-3-hydroxybutyrate accumulation in Escherichia coli Data from enzymatic assays and oxygen-limited continuous cultures
Data Brief
33
106588
2020
Candidatus Accumulibacter phosphatis (C7RM91), Candidatus Accumulibacter phosphatis UW-1 (C7RM91), Cupriavidus necator
brenda
Singh, A.; Das, M.; Grover, A.
Molecular mechanism of acetoacetyl-CoA enhanced kinetics for increased bioplastic production from Cupriavidus necator 428
J. Biomol. Struct. Dyn.
38
827-840
2020
Cupriavidus necator (P14697), Cupriavidus necator DSM 428 (P14697)
brenda
Pu, N.; Wang, M.R.; Li, Z.J.
Characterization of polyhydroxyalkanoate synthases from the marine bacterium Neptunomonas concharum JCM17730
J. Biotechnol.
319
69-73
2020
Neptunomonas concharum (A0A5P1R8U8 and A0A5P1RES5), Neptunomonas concharum, Neptunomonas concharum JCM17730 (A0A5P1R8U8 and A0A5P1RES5), Neptunomonas concharum JCM17730
brenda
Olavarria, K.; Carnet, A.; van Renselaar, J.; Quakkelaar, C.; Cabrera, R.; Guedes da Silva, L.; Smids, A.L.; Villalobos, P.A.; van Loosdrecht, M.C.M.; Wahl, S.A.
An NADH preferring acetoacetyl-CoA reductase is engaged in poly-3-hydroxybutyrate accumulation in Escherichia coli
J. Biotechnol.
325
207-216
2021
Candidatus Accumulibacter phosphatis (C7RM91), Candidatus Accumulibacter phosphatis UW-1 (C7RM91)
brenda
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