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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3R)-3-hydroxydecanoyl-CoA + NADP+
3-oxodecanoyl-CoA + NADPH + H+
-
(3R)-hydroxyacyl-CoA dehydrogenase
-
-
?
(3R)-hydroxybutyryl-CoA + NAD+
3-oxobutylryl-CoA + NADH
-
-
-
-
?
(3R)-hydroxybutyryl-CoA + NADP+
3-oxobutyryl-CoA + NADPH + H+
-
-
-
-
?
(3R)-hydroxydecanoyl-CoA + NAD+
3-oxodecanoyl-CoA + NADH
-
-
-
-
?
(3R)-hydroxyhexadecanoyl-CoA + NADP+
3-oxohexadecanoyl-CoA + NADPH + H+
-
-
-
-
?
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA
trans-2-butenoyl-CoA + H2O
-
dehydration, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
3-oxobutyryl-CoA + NADH + H+
-
-
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
oxidation, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NADPH + H+
3-oxobutyryl-CoA + NADP+
-
-
-
-
r
(R)-3-hydroxydecanoyl-CoA + NAD+
3-oxodecanoyl-CoA + NADH + H+
-
-
-
-
?
2-methylacetoacetyl-CoA + NADPH
2-methyl-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
? + NADPH
(R)-3-hydroxybutyrylphosphopantetheine + NADP+
-
-
-
?
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
D-3-hydroxybutyryl-CoA + NAD+
-
PHA-synthesis
-
ir
acetoacetyl-CoA + NADH + H+
D-beta-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
L-beta-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADPH
?
-
biosynthesis of poly(D-3-hydroxybutyrate)
-
-
?
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutanoyl-CoA +NADP+
-
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
acetoacetyl-pantetheine + NADPH + H+
D-3-hydroxybutyryl-pantetheine + NADP+
-
-
-
-
r
acetoacetyl-S-(D-pantetheine)11-pivalate + NADPH
3-hydroxybutyryl-S-(D-pantetheine)11-pivalate + NADP+
-
-
-
?
beta-ketopalmitoyl-CoA + ?
?
-
-
-
?
butyrylacetyl-CoA + NADPH
3-hydroxyhexanoyl-CoA + NADP+
-
-
-
?
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
D-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
-
-
-
r
pantetheine 11-pivalate + ?
?
-
-
-
-
?
propionylacetyl-CoA + NADPH
3-hydroxypentanoyl-CoA + NADP+
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
additional information
?
-
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
-
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
-
-
-
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
D-beta-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
D-beta-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
low activity
-
r
acetoacetyl-CoA + NADH + H+
L-beta-hydroxybutyryl-CoA + NAD+
-
reverse only with L-form
-
r
acetoacetyl-CoA + NADH + H+
L-beta-hydroxybutyryl-CoA + NAD+
-
reverse only with L-form
-
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
ir
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
Pigeon
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
Pigeon
-
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
ir
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
step in the biosynthesis of polyhydroxybutyrate, a biodegradable thermoplastic polymer
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
step in the enzyme-catalyzed synthesis system for production of poly(3-hydroxybutyrate) in vitro, overview
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
high activity
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
r
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
reverse only with D-form
-
r
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
-
reverse only with D-form
-
r
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
Pigeon
-
-
-
ir
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
-
-
-
?
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
Pigeon
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
-
-
-
-
?
additional information
?
-
-
KCR catalyzes the first reduction during elongation of very-long-chain fatty acids, VLCFA, precursors of sphingolipids, triacylglycerols, cuticular waxes, and suberin in plants
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no oxidation of (R/S)-3-hydroxybutyryl-CoA is detected when using NADP+ as cofactor
-
-
-
additional information
?
-
no oxidation of (R/S)-3-hydroxybutyryl-CoA is detected when using NADP+ as cofactor
-
-
-
additional information
?
-
no activity is detected when NADPH is replaced by NADH
-
-
-
additional information
?
-
-
no activity is detected when NADPH is replaced by NADH
-
-
-
additional information
?
-
no activity is detected when NADPH is replaced by NADH
-
-
-
additional information
?
-
Pigeon
-
-
-
-
?
additional information
?
-
Pigeon
-
not: crotonyl-CoA
-
-
?
additional information
?
-
Pigeon
-
not: octanoyl-CoA
-
-
?
additional information
?
-
Pigeon
-
not: beta-hydroxybutyryl-CoA
-
-
?
additional information
?
-
-
a point mutation in the dehydrogenase region of the enzyme causes peroxisomal disease leading to severe abnormalities and an early death
-
-
?
additional information
?
-
-
not: crotonyl-CoA
-
-
?
additional information
?
-
-
poor substrate: D-3-hydroxyvaleryl-CoA
-
-
?
additional information
?
-
-
not: L-3-hydroxyacyl-CoA
-
-
?
additional information
?
-
-
not: D-3-hydroxyacyl-CoA's with chain length exceeding 6
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA
trans-2-butenoyl-CoA + H2O
-
dehydration, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
oxidation, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NADPH + H+
3-oxobutyryl-CoA + NADP+
-
-
-
-
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
D-3-hydroxybutyryl-CoA + NAD+
-
PHA-synthesis
-
ir
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADPH
?
-
biosynthesis of poly(D-3-hydroxybutyrate)
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
additional information
?
-
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
-
r
(R)-3-hydroxyacyl-CoA + NADP+
3-oxoacyl-CoA + NADPH + H+
-
-
-
-
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
-
-
-
r
3-oxoacyl-CoA + NADPH + H+
(R)-3-hydroxyacyl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
acetoacetyl-CoA + NADH + H+
(R)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
-
-
?
acetoacetyl-CoA + NADH + H+
L-3-hydroxybutyryl-CoA + NAD+
-
low activity
-
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
step in the biosynthesis of polyhydroxybutyrate, a biodegradable thermoplastic polymer
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
r
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
FabG1 exhibits NADPH-dependent activity of acetoacetyl-CoA reductase
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
tricarboxylic acid cycle, poly-3-hydroxybutyrate synthesis, aerobic serine pathway
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
high activity
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
?
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
-
PHB synthesis
-
r
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
-
-
-
?
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
-
-
-
-
?
additional information
?
-
-
KCR catalyzes the first reduction during elongation of very-long-chain fatty acids, VLCFA, precursors of sphingolipids, triacylglycerols, cuticular waxes, and suberin in plants
-
-
?
additional information
?
-
-
a point mutation in the dehydrogenase region of the enzyme causes peroxisomal disease leading to severe abnormalities and an early death
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-
?
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A+/B+CtMFE-2(h2delta)
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recombinant enzyme
A-/B+CtMFE-2(hdelta2deltaadelta)
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domain A deleted
A-/B-CtMFE-2(hdelta2deltabdelta)
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domain A and B deleted
Q47L
-
the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
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T173S
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the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
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Q47L
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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
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D370A
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site-directed mutagenesis
D490A
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site-directed mutagenesis
D510A
-
site-directed mutagenesis, inactive
D517A
-
site-directed mutagenesis
E366A
-
site-directed mutagenesis, kcat/Km 100times lower than that of the wild type
E408A
-
site-directed mutagenesis
G16S
-
site-directed mutagenesis
H406A
-
site-directed mutagenesis
H515A
-
site-directed mutagenesis
H532A
-
site-directed mutagenesis
Y347A
-
site-directed mutagenesis
Y410A
-
site-directed mutagenesis
Y505A
-
site-directed mutagenesis
G16S
-
site-directed mutagenesis
G329S
-
site-directed mutagenesis
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
by random mutagenesis and high-throughput screening, enzyme mutant engineering for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system
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
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
-
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
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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
-
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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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
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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
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expressed in Brassica napus, transported with fusion peptide to seed leukoplast
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expressed in Escherichia coli
-
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
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli JM155
-
expressed in Escherichia coli strain JM109
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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
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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Qin, Y.M.; Poutanen, M.H.; Helander, H.M.; Kvist, A.P.; Siivari, K.M.; Schmitz, W.; Conzelmann, E.; Hellman, U.; Hiltunen, J.K.
Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization
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Rattus norvegicus
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An NADP-linked acetoacetyl CoA reductase from Zoogloea ramigera
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Streptomyces coelicolor
-
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246
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Pigeon, Zoogloea ramigera
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Cupriavidus necator, Azotobacter beijerinckii, Syntrophomonas wolfei, Zoogloea ramigera
-
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156
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Azotobacter vinelandii, Cupriavidus necator, Methylorubrum extorquens, Methylorubrum rhodesianum, Rhodospirillum rubrum, Zoogloea ramigera, Methylorubrum extorquens 15, Methylorubrum rhodesianum MB 126
-
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Methylobacterium rhodesianum MB 126 possesses two acetoacetyl-CoA reductases
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Methylorubrum rhodesianum, Rhodococcus ruber, Rhodospirillum rubrum, Zoogloea ramigera, Methylorubrum rhodesianum MB 126
-
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Gerngross, T.U.; Martin, D.P.
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92
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Cupriavidus necator
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Poly(beta-hydroxybutyrate) production in oilseed leukoplasts of Brassica napus
Planta
209
547-550
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Cupriavidus necator
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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
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4965-4972
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Homo sapiens
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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
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324
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Candida tropicalis
brenda
Satoh, Y.; Tajima, K.; Tannai, H.; Munekata, M.
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95
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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
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165
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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
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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)
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Aeromonas hydrophila, Cupriavidus necator
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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
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71
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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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Aeromonas hydrophila, Pseudomonas putida, Aeromonas hydrophila 4AK4
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Candida tropicalis
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Cupriavidus necator, no activity in Escherichia coli, no activity in Escherichia coli DH5-alpha
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Cupriavidus necator
-
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Hiltunen, J.K.; Wenzel, B.; Beyer, A.; Erdmann, R.; Fossa, A.; Kunau, W.H.
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-
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brenda
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77
54-60
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Rickettsia felis (Q4UN54), Rickettsia felis, Rickettsia felis ATCC VR-1525 (Q4UN54)
brenda
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474
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Mycolicibacterium smegmatis (A0R723), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2155 (A0R723)
brenda
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NADH-driven poly-3-hydroxybutyrate accumulation in Escherichia coli Data from enzymatic assays and oxygen-limited continuous cultures
Data Brief
33
106588
2020
Cupriavidus necator, Candidatus Accumulibacter phosphatis (C7RM91), Candidatus Accumulibacter phosphatis UW-1 (C7RM91)
brenda
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38
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Cupriavidus necator (P14697), Cupriavidus necator DSM 428 (P14697)
brenda
Pu, N.; Wang, M.R.; Li, Z.J.
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J. Biotechnol.
319
69-73
2020
Neptunomonas concharum (A0A5P1R8U8 and A0A5P1RES5), Neptunomonas concharum, Neptunomonas concharum JCM17730 (A0A5P1R8U8 and A0A5P1RES5), Neptunomonas concharum JCM17730
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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
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325
207-216
2021
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