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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 + 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-hydroxyhexanoyl-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 + H+
(S)-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 + H+
-
-
-
-
?
17beta-estradiol + NAD+
estrone + NADH + H+
-
enzyme from brain contains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH + H+
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
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 + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
both enzyme activities are specific for L-isomers
-
r
acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
both enzyme activities are specific for L-isomers
-
r
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
-
-
-
-
?
acetoacetyl-CoA + NADH + H+
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 + H+
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 + H+
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
17beta-estradiol + NAD+
estrone + NADH + H+
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH + H+
-
inactivation
-
-
?
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
-
-
?
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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
-
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
-
metabolism
-
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
-
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
-
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
-
the enzyme is involved in benzoyl-coenzyme A degradation
-
metabolism
-
the enzyme is involved in beta-oxidation cycle
-
metabolism
-
the enzyme is involved in fatty acid degradation metabolism
-
metabolism
-
the enzyme specifically catalyzes the third step of beta oxidation
-
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
-
physiological function
-
PaaH functions as an NAD+-dependent [probably (S)-3specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
physiological function
-
PaaH functions as an NAD+-dependent [probably (S)-3specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
physiological function
-
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
-
PaaH functions as an NAD+-dependent [probably (S)-3specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
-
physiological function
-
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
physiological function
-
the enzyme is involved in autotrophic carbon fixation
-
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
-
additional information
-
enzyme-protein interaction analysis in different tissues and subcellular compartments, detailed overview
additional information
conserved catalytic residues are Ser119, His140, and Asn190
additional information
-
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
-
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
-
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
-
the adenosine diphosphate moiety of NAD+ is not highly stabilized compared with the remainder of the acetoacetyl-CoA molecule
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
-
conserved catalytic residues are Ser119, His140, and Asn190
-
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purified recombinant detagged enzyme, hanging drop vapour diffusion method, 10 mg/ml protein in 25 mM sodium acetate trihydrate, pH 5.0, and 300 mM sodium chloride is mixed with an equal volume of reservoir solution, containing 21% PEG 3350, 0.2 M sodium chloride, 0.1 M MES, pH 6.5, for parallelepiped-shaped crystals and 23% PEG 3350, 0.2 M sodium chloride, 0.1 M bicine, pH 8.0, for cuboid-shaped crystals, equilibration against 0.20 ml reservoir solution, 3-5days at 18°C, X-ray diffraction structure determination and analysis of parallelepiped-shaped cuboid-shaped crystal at 1.60 A and 2.20 A resolution, respectively
purified recombinant detagged wild-type enzyme, crystals are grown by hanging drop method from 23% PEG 3350, 0.2 M sodium chloride, 0.1M N,N-bis (2-hydroxyethyl)glycine, pH 8.0, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement with the human HAD structure as search model, PDB ID 3had
apoenzyme, hanging drop vapor diffusion method, using 1.25% (w/v) PEG 400, 2.2 M ammonium sulfate, 0.1 M HEPES-NaOH pH 7.5. Enzyme in complex with NAD+, hanging drop vapor diffusion method, using 17.5% (w/v) PEG 3350, 200 mM sodium thiocyanate
-
hanging drop vapour diffusion method, mixing of 30 mg/ml protein in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 2 M ammonium sulfate, 0.1 M CAPS, pH 10.5, and 0.2 M lithium sulfate, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method and structure modeling
purified recombinant His6-tagged wild-type enzyme in apoform and in complex with substrates acetoacetyl-CoA and NAD+, hanging drop vapour diffusion method, mixing of 30 mg/ml protein in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with or without 20 mM NAD+, and 20 mM acetoacetyl-CoA, with reservoir solution containing 0.2 M Li2SO4, 0.1 M CAPS, pH 10.5, and 2 M ammonium sulfate, 22°C, 7 days, X-ray diffraction structure determination and analysis at 1.8-2.54 A resolution, molecular replacement and structure modeling
purified recombinant enzyme in apoform, as selenomethionine-labeled enzyme, and in complex with substrates acetoacetyl-CoA and NAD+, hanging drop vapour diffusion method, mixing of 50 mg/ml wild-type protein or selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 2 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.42-2.7 A resolution, molecular replacement using the crystal structure of the apo-form of RePaaH1, and structure modeling
purified recombinant wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of 30 mg/ml wild-type protein or 25 mg/ml selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 1.4 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.0, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, single-wavelength anomalous dispersion method
50 mM N(2-acetamido)-2-iminodiacetic acid, pH 6.5, polyethylene glycol 4000, 5 mM NAD+ hanging drop, crystals within 3 to 5 days at 18°C, enzyme structure is compromised of two domains, a NAD+-binding domain and a helical C-terminal domain
-
50% saturation with ammonium sulfate solution, 0.1 M potassium phosphate, pH 6.8, 1 mM EDTA, 2 mM beta-mercaptoethanol, 4°C, crystals appear after 2 days
-
dialysis against 40% saturated ammonium sulfate containing 100 mM phosphate, 2 mM beta-mercaptoethanol, 1 mM EDTA, pH 6.9, 7.5 or 8.2, vapor diffusion crystallization, crystals are obtained in the ammonium sulfate saturation range of 41% to 48%
-
polyethylene glycol, pH 8, orthorhombic crystals, 2.7 A resolution, crystallisation at pH 5 leads to trigonal space group
-
two dimers of the enzyme in the asymmetric unit of an orthorombic cell, two coenzyme binding sites per dimer
-
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R204A
site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
R204A/Y209A
site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
Y209A
site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
H138A
-
the mutant shows a slightly lower Km value and a significantly lower kcat value than the wild type enzyme
N188A
-
the mutation abolishes the activity of the enzyme
S117A
-
the mutation abolishes the activity of the enzyme
K50A
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
K50A//L232Y
site-directed mutagenesis, the mutant shows about 3fold increased activity compared to the wild-type enzyme
K50A/K54
site-directed mutagenesis, the mutant shows about 3fold increased activity compared to the wild-type enzyme
K50A/K54A/L232Y
site-directed mutagenesis, the mutant shows about 5fold increased activity compared to the wild-type enzyme
K54A
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
K54A/L232Y
site-directed mutagenesis, the mutant shows about 4fold increased activity compared to the wild-type enzyme
L232Z
site-directed mutagenesis, the mutant shows about 2.5fold increased activity compared to the wild-type enzyme
K56A
site-directed mutagenesis, the mutant shows about twofold increased activity compared to the wild-type enzyme
N190A
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
R52A
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
S119A
site-directed mutagenesis, almost inactive mutant
K56A
-
site-directed mutagenesis, the mutant shows about twofold increased activity compared to the wild-type enzyme
-
N190A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
-
R52A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
-
S119A
-
site-directed mutagenesis, almost inactive mutant
-
D279E
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
D45G/Y214H
a naturally occuring enzyme mutation causing human disease
H152Q
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
M176V
a naturally occuring enzyme mutation causing human disease
M188V
naturally occuring enzyme mutation, clinical data, overview
P246L
a naturally occuring enzyme mutation causing human disease
P258L
naturally occuring enzyme mutation, clinical data, overview
P86L
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
R224X
a naturally occuring enzyme mutation causing human disease
R236X
naturally occuring enzyme mutation, clinical data, overview
N208A
-
site-directed mutagenesis, the substrate binding of the mutant enzyme is affected
S137C
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S137T
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S137A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S137A
-
site-directed mutagenesis, the substrate binding of the mutant enzyme is affected
additional information
-
loss of KCR1 function results in embryo lethality, which cannot be rescued by KCR2 expression using the KCR1 promoter. Disruption of the KCR2 gene has no obvious phenotypic effect
additional information
structure-based protein engineering of CbHBD for increasing the production rate of n-butanol in biofuel production
additional information
-
structure-based protein engineering of CbHBD for increasing the production rate of n-butanol in biofuel production
additional information
-
inactivation of the enzyme by siRNA expression, the mutants show reduced beta-oxidation of fatty acids
additional information
c.547-3_549delbis and IVS6-2a.gc are naturally occuring enzyme mutations causing human disease. Mapping of disease-relevant HAD mutations onto the crystal structure of human HAD, PDB ID 1F0Y
additional information
-
c.547-3_549delbis and IVS6-2a.gc are naturally occuring enzyme mutations causing human disease. Mapping of disease-relevant HAD mutations onto the crystal structure of human HAD, PDB ID 1F0Y
additional information
identified naturally occuring enzyme mutations are P258L, c.547-3_549del, c.547-3_549del, IVS6-2a>g, M188V, R236X, c.587delC, c.587delC, C.587delC, and c.261+IG>A from human hyperinsulinemic hypoglycemia patients, clinical data, overview
additional information
-
identified naturally occuring enzyme mutations are P258L, c.547-3_549del, c.547-3_549del, IVS6-2a>g, M188V, R236X, c.587delC, c.587delC, C.587delC, and c.261+IG>A from human hyperinsulinemic hypoglycemia patients, clinical data, overview
additional information
-
generation of hadh knockout mice by insertion of gene-trap vector pGT0Lxf in the ES cell line E14Tg2a.4, deletion of hadh results in a defective enzymatic activity of SCHAD, phenotype, overview. Deletion of hadh reduces body weight and adipose tissue depots, and leads to impaire thermogenesis
additional information
-
His-tagged SCHAD is immobilized on agarose beads, and interacting proteins from murine tissue extracts are isolated using affinity chromatography in preparation for LC-MS/MS identification, use of tissues from both wild-type and SCHAD knockout mice, protein interaction analysis using yeast-2 hybrid analysis and by pulldown assay, overview
additional information
-
construction of a deletion mutant of gene fadB encoding the enzyme, the mutant shows decreased production of medium-chain-length polyhydroxyalkanoates, e.g. of 3-hydroxyhexanoate, 3- hydroxyoctanoate, 3-hydroxydecanoate, 3-hydroxydodecanoate, and 3-hydroxytetradecanoate, overview
additional information
-
no extracellular 3-hydroxyalkanoic acid is produced by wild-type Pseudomonas putida KT2442 or the polyhydroxyalkanoate synthesis operon knockout mutant KTOY01 when lauric acid is used as carbon source. By expressing tesB gene encoding thioesterase II, Pseudomonas putida KT2442 can not produce extracellular 3-hydroxyalkanoic acid monomer, while the polyhydroxyalkanoate operon knockout mutant Pseudomonas putida KTOY01 (pSPD09) produces 0.35 g/l extracellular medium-chain-length 3-hydroxyalkanoic acid. KTOY07 is constructed by further knocking out fadB and fadA genes in Pseudomonas putida KTOY01. As a result, Pseudomonas putida KTOY07 increases medium-chain-length 3-hydroxyalkanoic acid to 1.68 from 0.35 g/l produced by the beta-oxidation intact mutant Pseudomonas putida KTOY01
additional information
-
construction of a deletion mutant of gene fadB encoding the enzyme, the mutant shows decreased production of medium-chain-length polyhydroxyalkanoates, e.g. of 3-hydroxyhexanoate, 3- hydroxyoctanoate, 3-hydroxydecanoate, 3-hydroxydodecanoate, and 3-hydroxytetradecanoate, overview
-
additional information
-
inactivation of the enzyme by siRNA expression, the mutants show reduced beta-oxidation of fatty acids, shRNA-mediated HADHSC silencing affects induced absolute and fractional insulin secretion in INS1 832-13 cells and the cellular insulin content, overview
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Leptospira interrogans serovar Copenhageni (Q72M90), Leptospira interrogans serovar Copenhageni Fiocruz LV4231 (Q72M90)
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Heslegrave, A.; Hussain, K.
Novel insights into fatty acid oxidation, amino acid metabolism, and insulin secretion from studying patients with loss of function mutations in 3-hydroxyacyl-CoA dehydrogenase
J. Clin. Endocrinol. Metab.
98
496-501
2013
Homo sapiens (Q16836), Homo sapiens
brenda
Kim, E.J.; Kim, J.; Ahn, J.W.; Kim, Y.J.; Chang, J.H.; Kim, K.J.
Crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium butyricum and its mutations that enhance reaction kinetics
J. Microbiol. Biotechnol.
24
1636-1643
2014
Clostridium butyricum (C4IEM5), Clostridium butyricum
brenda
Xu, Y.; Li, H.; Jin, Y.H.; Fan, J.; Sun, F.
Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate
PLoS ONE
9
e95965
2014
Caenorhabditis elegans (P34439), Caenorhabditis elegans, Homo sapiens (Q16836), Homo sapiens
brenda
Takenoya, M.; Taguchi, S.; Yajima, S.
Crystal structure and kinetic analyses of a hexameric form of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium acetobutylicum
Acta Crystallogr. Sect. F
74
733-740
2018
Clostridium acetobutylicum
brenda
Toma, C.; Koizumi, N.; Kakita, T.; Yamaguchi, T.; Hermawan, I.; Higa, N.; Yamashiro, T.
Leptospiral 3-hydroxyacyl-CoA dehydrogenase as an early urinary biomarker of leptospirosis
Heliyon
4
e00616
2018
Leptospira interrogans, Leptospira interrogans UP-MMC-NIID
brenda
Segawa, M.; Wen, C.; Orita, I.; Nakamura, S.; Fukui, T.
Two NADH-dependent (S)-3-hydroxyacyl-CoA dehydrogenases from polyhydroxyalkanoate-producing Ralstonia eutropha
J. Biosci. Bioeng.
127
294-300
2019
Cupriavidus necator
brenda