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(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
(R)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
cf. EC 1.1.1.36
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
3-oxobutyryl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
(S)-3-hydroxydecanoyl-CoA + ?
3-oxodecanoyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxydecanoyl-CoA + NAD+
3-ketodecanoyl-CoA + NADH
(S)-3-hydroxyhexanoyl-CoA + NAD+
3-oxohexanoyl-CoA + NADH + H+
(S)-3-hydroxyhexenoyl-CoA + NAD+
3-ketohexenoyl-CoA + NADH
-
-
-
r
(S)-3-hydroxylauryl-CoA + NAD+
3-oxolauryl-CoA + NADH
-
-
-
r
1-propanol + NAD+
n-propanal + NADH
-
multifunctional enzyme from brain
-
ir
17beta-estradiol + NAD+
estrone + NADH
17beta-estradiol + NAD+
estrone + NADH + H+
2-fluoro-3-hydroxy-4-octenoyl-CoA + NAD+
2-fluoro-3-oxo-4-octenoyl-CoA + NADH
-
-
-
-
r
2-fluoro-3-hydroxyoctanoyl-CoA + NAD+
2-fluoro-3-oxooctanoyl-CoA + NADH
-
-
-
-
r
2-propanol + NAD+
acetone + NADH
-
multifunctional enzyme from brain
-
ir
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
-
-
-
-
?
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
highest activity
-
-
?
3-hydroxy-2-methylacyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
-
preferred substrate of SCHAD, no activity towards 3-hydroxy-2-methylacyl-CoA by HAD
-
-
?
3-hydroxy-4-octenoyl-CoA + NAD+
3-oxo-4-octenoyl-CoA + NADH
-
-
-
-
r
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
3-hydroxyoctanoyl-CoA + NAD+
3-oxooctanoyl-CoA + NADH
-
-
-
-
r
3-ketohexadecanoyl-CoA + NADH
(S)-3-hydroxhexadecanoyl-CoA + NAD+
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
3-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
-
key enzyme involved in fatty acid oxidation
-
-
r
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxyacyl-CoA + NAD+
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
3-oxohexadecanoyl-CoA + NADH + H+
(S)-3-hydroxhexadecanoyl-CoA + NAD+
-
-
-
-
?
3-oxohexanoyl-CoA + NADH + H+
(S)-3-hydroxhexanoyl-CoA + NAD+
-
-
-
-
?
3-oxooctanoyl-CoA + NADH + H+
(S)-3-hydroxyoctanoyl-CoA + NAD+
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
5alpha-dihydrotestosterone + NADH
(3beta,5alpha,17beta)-androstane-3,17-diol + NAD+
-
-
-
r
8-(acetoacetylthio)-6-ethyloctanoic acid + NADH
6-ethyl-8-[[(1S)-1-hydroxy-3-oxobutyl]thio]octanoic acid + NAD+
-
-
-
r
8-(acetoacetylthio)-6-mercaptooctanoic acid + NADH
8-[[(1S)-1-hydroxy-3-oxobutyl]thio]-6-mercaptooctanoic acid + NAD+
-
-
-
r
acetoacetyl-CoA + NADH
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NADH
(S)-3-hydroxybutyryl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NAD+
-
-
-
r
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
acetoacetyl-N-beta-alanylcysteamine + NADH
(S)-3-hydroxybutyryl-N-beta-alanylcysteamine + NAD+
-
-
-
r
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
acetoacetyl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NADH
(S)-3-hydroxybutyryl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NAD+
-
-
-
r
acetoacetyldecanoate + NADH
(S)-3-hydroxybutyryldecanoate + NAD+
-
-
-
r
allopregnanolone + NAD+
5alpha-dihydroprogesterone + NADH
androsterone + NAD+
androstanedione + NADH
-
-
-
ir
tiglyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
-
activity of SCHAD
-
-
?
additional information
?
-
(3S)-3-hydroxyadipyl-CoA + NAD+

3-oxoadipyl-CoA + NADH + H+
-
-
-
-
?
(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
-
-
-
-
?
(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+

3-oxoacyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is a B-side-specific dehydrogenase with hydride transfer occurring on the si face of the nicotinamide ring
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+

acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
enzyme FadB' converts (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA, while no conversion of (R)-3-hydroxybutyryl-CoA is detected
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
substrates binding structure analysis, overview. The acetoacetyl-CoA substrate is positioned within the deep cleft between the N-terminal domain and C-terminal domain. The acetoacetyl moiety is positioned near the conserved catalytic residues Ser119, His140, and Asn190
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
substrates binding structure analysis, overview. The acetoacetyl-CoA substrate is positioned within the deep cleft between the N-terminal domain and C-terminal domain. The acetoacetyl moiety is positioned near the conserved catalytic residues Ser119, His140, and Asn190
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
enzyme FadB' converts (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA, while no conversion of (R)-3-hydroxybutyryl-CoA is detected
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
no activity with (R)-3-hydroxybutanoyl-CoA, no activity with NADP+. Bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
no activity with (R)-3-hydroxybutanoyl-CoA, no activity with NADP+. Bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
-
-
?
(S)-3-hydroxybutanoyl-CoA + NADP+

acetoacetyl-CoA + NADPH + H+
relative activity of FadB' measured with NADP+ is less than 10% in comparison to the activity measured with NAD+
-
-
?
(S)-3-hydroxybutanoyl-CoA + NADP+
acetoacetyl-CoA + NADPH + H+
relative activity of FadB' measured with NADP+ is less than 10% in comparison to the activity measured with NAD+
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+

3-acetoacetyl-CoA + NADH + H+
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
no activity woth NADP+
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
no activity woth NADP+
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+

acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
highest activity with acetoacetyl-CoA, significant activity with increasing chain length up to C16
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NADP+

acetoacetyl-CoA + NADPH
-
-
-
?
(S)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
-
low activity for mitochondrial enzyme
-
r
(S)-3-hydroxydecanoyl-CoA + NAD+

3-ketodecanoyl-CoA + NADH
-
-
-
?
(S)-3-hydroxydecanoyl-CoA + NAD+
3-ketodecanoyl-CoA + NADH
-
-
-
r
(S)-3-hydroxyhexanoyl-CoA + NAD+

3-oxohexanoyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyhexanoyl-CoA + NAD+
3-oxohexanoyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxyhexanoyl-CoA + NAD+
3-oxohexanoyl-CoA + NADH + H+
-
-
-
r
17beta-estradiol + NAD+

estrone + NADH
-
enzyme from brain contains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+

estrone + NADH + H+
-
-
-
-
?
17beta-estradiol + NAD+
estrone + NADH + H+
-
inactivation
-
-
?
3-acetoacetyl-CoA + NADH + H+

(S)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
3-acetoacetyl-CoA + NADPH + H+

(S)-3-hydroxybutyryl-CoA + NAD+
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
-
-
ir
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
-
-
ir
3-hydroxybutyryl-CoA + NAD+

acetoacetyl-CoA + NADH
-
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-ketohexadecanoyl-CoA + NADH

(S)-3-hydroxhexadecanoyl-CoA + NAD+
-
-
r
3-ketohexadecanoyl-CoA + NADH
(S)-3-hydroxhexadecanoyl-CoA + NAD+
-
-
-
r
3-ketooctanoyl-CoA + NADH

(S)-3-hydroxyoctanoyl-CoA + NAD+
-
-
-
?
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
-
-
r
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
-
-
-
?
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
-
-
-
r
3-oxoacyl-CoA + NADH + H+

(S)-3-hydroxyacyl-CoA + NAD+
-
-
-
-
?
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxyacyl-CoA + NAD+
-
-
-
-
?
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxyacyl-CoA + NAD+
-
-
-
-
?
3-oxofumonisin B3 + NADPH

fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
3-keto reduction
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
3-keto reduction
-
-
?
3-oxooctanoyl-CoA + NADH + H+

(S)-3-hydroxyoctanoyl-CoA + NAD+
-
-
-
-
?
3-oxooctanoyl-CoA + NADH + H+
(S)-3-hydroxyoctanoyl-CoA + NAD+
-
-
-
-
?
5alpha-androstane-3,17-diol + NAD+

5alpha-dihydrotestosterone + NADH
-
-
-
-
?
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
-
inactivation
-
-
?
acetoacetyl-CoA + NADH

(S)-3-hydroxybutyryl-CoA + NAD+
-
-
both enzyme activities are specific for L-isomers
-
r
acetoacetyl-CoA + NADH
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
both enzyme activities are specific for L-isomers
-
r
acetoacetyl-CoA + NADH

3-hydroxybutyryl-CoA + NAD+
-
for the purpose of specifically measuring intracellular Hadh2 activities, branched-chain acyl-CoA thioesters, instead of acetoacetyl-CoA, shall be used as the substrate in either the forward or reverse reaction. In contrast to 3-hydroxyacyl-CoA dehydrogenase catalyzing the third reaction of straight-chain fatty acid oxidation spiral, HSD10 (formerly Hadh2) functions in isoleucine and steroid metabolism
-
-
?
acetoacetyl-CoA + NADH
3-hydroxybutyryl-CoA + NAD+
-
-
-
-
r
acetoacetyl-N-acetylcysteamine + NADH

(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
-
?
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
?
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
-
?
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
r
acetoacetyl-pantetheine + NADH

(S)-3-hydroxybutyryl-pantetheine
-
-
-
-
?
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
-
-
-
-
?
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
-
-
-
?
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
-
-
-
-
?
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
-
-
-
r
allopregnanolone + NAD+

5alpha-dihydroprogesterone + NADH
-
-
-
-
?
allopregnanolone + NAD+
5alpha-dihydroprogesterone + NADH
-
inactivation
-
-
?
additional information

?
-
-
KCR1 can complement the yeast ybr159DELTA mutant, KCR proteins are divergent, only KCR1 can restore heterologous elongase activity, thus only KCR1 is a functional KCR isoform involved in microsomal fatty acid elongation
-
-
?
additional information
?
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
?
additional information
?
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
?
additional information
?
-
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
?
additional information
?
-
the N-terminal part of FadB' comprises an NAD+ binding site and is responsible for 3-hydroxyacyl-CoA dehydrogenase activity converting (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA. FadB' is strictly stereospecific to (S)-3-hydroxybutyryl-CoA and to prefers NAD+. NADP(H) is utilized at a rate of less than 10% in comparison to activity with NAD(H)
-
-
?
additional information
?
-
-
the activity of enzymes PaaH1 and Had with NADPH is as low as 2.2% and 1.2%, respectively, of the respective activity with NADH
-
-
-
additional information
?
-
the N-terminal part of FadB' comprises an NAD+ binding site and is responsible for 3-hydroxyacyl-CoA dehydrogenase activity converting (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA. FadB' is strictly stereospecific to (S)-3-hydroxybutyryl-CoA and to prefers NAD+. NADP(H) is utilized at a rate of less than 10% in comparison to activity with NAD(H)
-
-
?
additional information
?
-
the enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview
-
-
?
additional information
?
-
-
the enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview
-
-
?
additional information
?
-
-
the enzyme is involved in intracrinology and is essential for the metabolism of isoleucine and branched-chain fatty acids
-
-
?
additional information
?
-
-
the enzyme is involved in the penultimate step in mitochondrial fatty acid oxidation and in development of type 2 diabetes
-
-
?
additional information
?
-
short-chain L-3-hydroxyacyl-CoA dehydrogenase shows a wide substrate spectrum including cholic acids, steroids, and fatty acids with a preference for short-chain methyl-branched acyl-CoAs, SCHAD might be identical with 17beta-hydroxysteroid dehyxrogenase in human mitochondria, overview
-
-
?
additional information
?
-
-
short-chain L-3-hydroxyacyl-CoA dehydrogenase shows a wide substrate spectrum including cholic acids, steroids, and fatty acids with a preference for short-chain methyl-branched acyl-CoAs, SCHAD might be identical with 17beta-hydroxysteroid dehyxrogenase in human mitochondria, overview
-
-
?
additional information
?
-
-
HADH gene with a novel homozygous missense mutation M188V. Mutations in the HADH gene are associated with significantly decreased short-chain L-HADH activity, mildly decreased medium- and long-chain L-HADH activity, protein-induced hyperinsulinemic hypoglycemia. Patients with hyperinsulinemic hypoglycemia due to HADH gene mutations may have normal acylcarnitines and urine organic acids
-
-
?
additional information
?
-
-
no activity of the wild-type enzyme with 2,2-difluoro-3-hydroxyoctanoyl-CoA and 2,2-difluoro-3-hydroxy-4-octenoyl-CoA, substrate specificity of wild-type and mutant enzymes, y, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
17beta-estradiol + NAD+
estrone + NADH
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH + H+
-
inactivation
-
-
?
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
-
-
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
3-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
-
key enzyme involved in fatty acid oxidation
-
-
r
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxyacyl-CoA + NAD+
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
-
inactivation
-
-
?
allopregnanolone + NAD+
5alpha-dihydroprogesterone + NADH
-
inactivation
-
-
?
additional information
?
-
(3S)-3-hydroxyadipyl-CoA + NAD+

3-oxoadipyl-CoA + NADH + H+
-
-
-
-
?
(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
-
-
-
-
?
(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+

3-oxoacyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+

acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+

3-acetoacetyl-CoA + NADH + H+
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+

acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
3-hydroxybutyryl-CoA + NAD+

acetoacetyl-CoA + NADH
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-oxoacyl-CoA + NADH + H+

(S)-3-hydroxyacyl-CoA + NAD+
-
-
-
-
?
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxyacyl-CoA + NAD+
-
-
-
-
?
3-oxoacyl-CoA + NADH + H+
(S)-3-hydroxyacyl-CoA + NAD+
-
-
-
-
?
3-oxofumonisin B3 + NADPH

fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
additional information

?
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
?
additional information
?
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
?
additional information
?
-
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
?
additional information
?
-
the enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview
-
-
?
additional information
?
-
-
the enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview
-
-
?
additional information
?
-
-
the enzyme is involved in intracrinology and is essential for the metabolism of isoleucine and branched-chain fatty acids
-
-
?
additional information
?
-
-
the enzyme is involved in the penultimate step in mitochondrial fatty acid oxidation and in development of type 2 diabetes
-
-
?
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.
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0.034
(3beta,5alpha,17beta)-androstane-3,17-diol
-
enzyme from brain
0.0505 - 0.1157
(R)-3-hydroxyacyl-CoA
0.06 - 0.2
(S)-3-hydroxybutanoyl-CoA
0.000058 - 43.5
(S)-3-hydroxybutyryl-CoA
0.088
(S)-3-hydroxydecanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxydecanoyl-CoA
0.0286 - 0.34
(S)-3-hydroxyhexanoyl-CoA
0.1
(S)-3-hydroxylauryl-CoA
-
-
0.0163 - 0.35
(S)-3-hydroxyoctanoyl-CoA
0.043
17beta-estradiol
-
enzyme from brain
0.0096 - 65.6
3-acetoacetyl-CoA
0.0094 - 0.0175
3-acetoacyl-CoA
-
0.0083 - 0.016
3-oxohexanoyl-CoA
0.0065 - 0.0125
3-oxooctanoyl-CoA
0.003 - 0.263
acetoacetyl-CoA
44.4
acetoacetyl-N-acetyl-cysteamine
-
-
10
acetoacetyl-N-acetylcysteamine
-
-
1.4
acetoacetyl-N-beta-alanylcysteamine
-
-
10
acetoacetyl-Nacetylcysteamine
-
-
0.08 - 1.19
acetoacetyl-pantetheine
0.045
androsterone
-
enzyme from brain
additional information
additional information
-
0.0505
(R)-3-hydroxyacyl-CoA

recombinant mutant Y209A, pH 7.0, 25ưC
0.0721
(R)-3-hydroxyacyl-CoA
recombinant wild-type enzyme, pH 7.0, 25ưC
0.0833
(R)-3-hydroxyacyl-CoA
recombinant mutant R204A, pH 7.0, 25ưC
0.1157
(R)-3-hydroxyacyl-CoA
recombinant mutant R204A/Y209A, pH 7.0, 25ưC
0.06
(S)-3-hydroxybutanoyl-CoA

pH 8.0, 70ưC
0.2
(S)-3-hydroxybutanoyl-CoA
pH 8.0, 65ưC
0.000058
(S)-3-hydroxybutyryl-CoA

-
isozyme SCHAD II, at pH 8.0
0.000058
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD II, at pH 9.3
0.00261
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD I, at pH 8.0
0.00529
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD I, at pH 8.5
0.0699
(S)-3-hydroxybutyryl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxybutyryl-CoA
0.31
(S)-3-hydroxybutyryl-CoA
-
-
43.5
(S)-3-hydroxybutyryl-CoA
pH 9.5, 30ưC
0.0286
(S)-3-hydroxyhexanoyl-CoA

-
mitochondrial enzyme, oxidation of (S)-3-hydroxyhexanoyl-CoA
0.34
(S)-3-hydroxyhexanoyl-CoA
-
-
0.0163
(S)-3-hydroxyoctanoyl-CoA

-
mitochondrial enzyme, oxidation of (S)-3-hydroxyoctanoyl-CoA
0.35
(S)-3-hydroxyoctanoyl-CoA
-
-
0.0096
3-acetoacetyl-CoA

-
mutant enzyme H138A, at pH 7.5 and 37ưC
0.0227
3-acetoacetyl-CoA
-
wild type enzyme, at pH 7.5 and 37ưC
65.6
3-acetoacetyl-CoA
pH 7.0, 30ưC
0.0094
3-acetoacyl-CoA

-
enzyme PaaH1, at pH 8.0 and 30ưC
-
0.0175
3-acetoacyl-CoA
-
enzyme Had, at pH 8.0 and 30ưC
-
0.0083
3-oxohexanoyl-CoA

-
enzyme PaaH1, at pH 8.0 and 30ưC
0.016
3-oxohexanoyl-CoA
-
enzyme Had, at pH 8.0 and 30ưC
0.0065
3-oxooctanoyl-CoA

-
enzyme Had, at pH 8.0 and 30ưC
0.0125
3-oxooctanoyl-CoA
-
enzyme PaaH1, at pH 8.0 and 30ưC
0.003
acetoacetyl-CoA

-
-
0.0138
acetoacetyl-CoA
-
pH 8.0
0.0166
acetoacetyl-CoA
-
isozyme SCHAD I, at pH 7.0
0.0169
acetoacetyl-CoA
-
-
0.01825
acetoacetyl-CoA
pH 8.0, 30ưC, recombinant enzyme
0.0187
acetoacetyl-CoA
-
pH 7.0
0.0222
acetoacetyl-CoA
-
isozyme SCHAD I, at pH 8.0
0.0257
acetoacetyl-CoA
-
isozyme SCHAD II, at pH 7.0
0.03
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137C
0.0315
acetoacetyl-CoA
-
isozyme SCHAD II, at pH 8.0
0.0345
acetoacetyl-CoA
-
pH 5.0
0.036
acetoacetyl-CoA
-
-
0.044
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged wild-type enzyme
0.045
acetoacetyl-CoA
-
pH 6.0
0.048
acetoacetyl-CoA
pH 6.5, 30ưC, recombinant enzyme
0.05
acetoacetyl-CoA
-
pH 6.5
0.066
acetoacetyl-CoA
-
-
0.076
acetoacetyl-CoA
pH 6.5, 30ưC, recombinant enzyme in presence of 0.1 mM acetyl-CoA
0.089
acetoacetyl-CoA
enzyme from brain
0.184
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137A
0.263
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137T
0.08
acetoacetyl-pantetheine

-
-
0.4
acetoacetyl-pantetheine
-
-
0.56
acetoacetyl-pantetheine
-
-
1.19
acetoacetyl-pantetheine
-
-
0.00009
NAD+

-
isozyme SCHAD II, at pH 7.0
0.00119
NAD+
-
isozyme SCHAD I, at pH 7.0
0.05
NAD+
-
enzyme from brain, substrate 17beta-estradiol
0.21
NAD+
-
enzyme from brain, substrate dihydroandrosterone
0.242
NAD+
-
enzyme from brain, substrate androsterone
0.25
NAD+
pH 8.0, 65ưC
29.5
NAD+
pH 9.5, 30ưC
0.0009
NADH

-
isozyme SCHAD II, at pH 9.3
0.0168
NADH
-
mutant enzyme H138A, at pH 7.5 and 37ưC
0.02
NADH
enzyme from brain
0.0314
NADH
-
wild type enzyme, at pH 7.5 and 37ưC
0.0338
NADH
-
isozyme SCHAD I, at pH 8.5
additional information
additional information

Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes, detailed overview
-
additional information
additional information
-
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes, detailed overview
-
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evolution

based on the chain length of the substrates, the HAD family is divided into three subclasses: 3-hydroxyacyl-CoA dehydrogenases (HADs), long-chain 3-hydroxyacyl-CoA dehydrogenases (LCHADs) and short-chain 3-hydroxyacyl-CoA dehydrogenases (SCHADs). HADs are soluble dimeric enzymes that exhibit substrate specificity for an acyl-chain length of C4-C10 and are previously referred to as short-chain HADs
evolution
Caenorhabditis elegans HAD is highly conserved to human HAD
evolution
Caenorhabditis elegans HAD is highly conserved to human HAD
evolution
two (S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratases, H16_A0461/FadB' and H16_A1526/FadB1, are involved in the FA degradation in Ralstonia eutropha H16. FadB' and FadB1 possess an enoyl-CoA hydratase activity, catalyzing hydrogenation of the unsaturated enoyl coenzyme A (CoA), and a 3-hydroxyacyl-CoA dehydrogenase activity, i.e. oxidation of the hydroxyl group into a keto group using one NAD+ molecule
evolution
-
two (S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratases, H16_A0461/FadB' and H16_A1526/FadB1, are involved in the FA degradation in Ralstonia eutropha H16. FadB' and FadB1 possess an enoyl-CoA hydratase activity, catalyzing hydrogenation of the unsaturated enoyl coenzyme A (CoA), and a 3-hydroxyacyl-CoA dehydrogenase activity, i.e. oxidation of the hydroxyl group into a keto group using one NAD+ molecule
-
malfunction

-
mice lacking SCHAD, hadh-/-, display a lower body weight and a reduced fat mass in comparison with hadh+/+ mice under high-fat diet conditions, presumably due to an impaired fuel efficiency, the loss of acylcarnitines via the urine, and increased body temperature. Food intake, total energy expenditure, and locomotor activity are not altered in knockout mice
malfunction
a null mutant of fadB2 shows no significant differences from the wild-type strain with regard to lipid composition, utilization of different fatty acid carbon sources and tolerance to various stresses
malfunction
mutantions with attenuated interactions on the dimerization interface significantly decrease the enzyme activity compared to the wild-type. Such reduced activities are in consistency with the reduced ratios of the catalytic intermediate formation. Further molecular dynamics simulations results reveal that the alteration of the dimerization interface will increase the fluctuation of a distal region that plays an important role in the substrate binding. The increased fluctuation decreases the stability of the catalytic intermediate formation, and therefore the enzymatic activity is attenuated
malfunction
mutations in HADH cause hyperinsulinemic hypoglycemia that is precipitated by protein in a similar manner to the hyperinsulinism/hyperammonemia (HI/HA) syndrome, which is caused by mutations in the GLUD1 gene, encoding the enzyme glutamate dehydrogenase (GDH), suggesting a link between mitochondrial fatty acid oxidation, amino acid metabolism, and insulin secretion, clinical phenotypes, overview
malfunction
numerous human diseases are found related to mutations at HAD dimerization interface that is away from the catalytic pocket
malfunction
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a null mutant of fadB2 shows no significant differences from the wild-type strain with regard to lipid composition, utilization of different fatty acid carbon sources and tolerance to various stresses
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metabolism

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the enzyme catalyzes the third reaction of the mitochondrial beta-oxidation cascade, the oxidation of 3-hydroxyacyl-CoA to 3-ketoacyl-CoA, for medium-andshort-chain fatty acids
metabolism
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the enzyme is the penultimate enzyme of mitochondrial fatty acid beta-oxidation
metabolism
the enzyme is involved in benzoyl-coenzyme A degradation
metabolism
the enzyme is involved in beta-oxidation cycle
metabolism
3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation
metabolism
3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation
metabolism
3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation, oxidizing the hydroxyl group of 3-hydroxyacyl-CoA to a keto group
metabolism
the enzyme catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to 3-hydroxybutyryl-CoA
metabolism
the enzyme catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to 3-hydroxybutyryl-CoA
metabolism
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the enzyme catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to 3-hydroxybutyryl-CoA
metabolism
the enzyme is involved in fatty acid degradation metabolism
metabolism
the enzyme specifically catalyzes the third step of beta oxidation
metabolism
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the enzyme is involved in benzoyl-coenzyme A degradation
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metabolism
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the enzyme specifically catalyzes the third step of beta oxidation
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metabolism
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the enzyme is involved in beta-oxidation cycle
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metabolism
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the enzyme is involved in fatty acid degradation metabolism
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metabolism
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the enzyme catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to 3-hydroxybutyryl-CoA
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physiological function

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PaaH functions as an NAD+-dependent [probably (S)-3Ć¢ĀĀspecific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
physiological function
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PaaH functions as an NAD+-dependent [probably (S)-3Ć¢ĀĀspecific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
physiological function
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the enzyme is involved in thermogenesis, in the maintenance of body weight, and in the regulation of nutrient-stimulated insulin secretion. It plays an important role in adaptive thermogenesis
physiological function
the enzyme is involved in autotrophic carbon fixation
physiological function
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
physiological function
important role for HADH in insulin secretion
physiological function
the enzyme is classified as an oxidoreductase in fatty acid metabolic processes. It specifically catalyzes the third step of beta oxidation. Long-chain fatty acids are utilized by Leptospira as the sole carbon source and are metabolized by beta-oxidation. Therefore, a large amount of HADH may be produced intracellularly and released to get carbons and energy by oxidizing free fatty acid
physiological function
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the enzyme is classified as an oxidoreductase in fatty acid metabolic processes. It specifically catalyzes the third step of beta oxidation. Long-chain fatty acids are utilized by Leptospira as the sole carbon source and are metabolized by beta-oxidation. Therefore, a large amount of HADH may be produced intracellularly and released to get carbons and energy by oxidizing free fatty acid
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physiological function
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PaaH functions as an NAD+-dependent [probably (S)-3Ć¢ĀĀspecific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
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physiological function
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the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
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physiological function
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the enzyme is involved in autotrophic carbon fixation
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additional information

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enzyme-protein interaction analysis in different tissues and subcellular compartments, detailed overview
additional information
conserved catalytic residues are Ser119, His140, and Asn190
additional information
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conserved catalytic residues are Ser119, His140, and Asn190
additional information
FadB' is an enzyme with two catalytic domains exhibiting a single monomeric structure and possessing a molecular weight of 86 kDa. The C-terminal part of the enzyme harbors enoyl-CoA hydratase activity, EC 4.2.1.17, and is able to convert trans-crotonyl-CoA to 3-hydroxybutyryl-CoA. The N-terminal part of FadB' comprises an NAD+ binding site and is responsible for 3-hydroxyacyl-CoA dehydrogenase activity converting (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA
additional information
molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects, molecular dynamics simulation, overview
additional information
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molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects, molecular dynamics simulation, overview
additional information
molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects, molecular dynamics simulation, overview
additional information
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molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects, molecular dynamics simulation, overview
additional information
the adenosine diphosphate moiety of NAD+ is not highly stabilized compared with the remainder of the acetoacetyl-CoA molecule
additional information
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the adenosine diphosphate moiety of NAD+ is not highly stabilized compared with the remainder of the acetoacetyl-CoA molecule
additional information
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FadB' is an enzyme with two catalytic domains exhibiting a single monomeric structure and possessing a molecular weight of 86 kDa. The C-terminal part of the enzyme harbors enoyl-CoA hydratase activity, EC 4.2.1.17, and is able to convert trans-crotonyl-CoA to 3-hydroxybutyryl-CoA. The N-terminal part of FadB' comprises an NAD+ binding site and is responsible for 3-hydroxyacyl-CoA dehydrogenase activity converting (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA
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additional information
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conserved catalytic residues are Ser119, His140, and Asn190
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