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Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase
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1.1.1.35 3-hydroxyacyl-CoA dehydrogenaseIUBMB Comments
Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
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Word Map
- 1.1.1.35
- citrate
- acyl-coas
-
thiolase
- peroxisomal
- carnitine
-
trifunctional
-
phosphofructokinase
- hexokinase
-
endurance
- lateralis
-
vastus
- soleus
-
medium-chain
- acetoacetyl-coa
- hypoglycemia
-
2-enoyl-coa
- acylcarnitines
- hyperinsulinism
-
extensor
- lchad
-
fast-twitch
-
plantaris
-
4.1.3.7
-
hypoketotic
- crotonase
- 3-oxoacyl-coa
-
hellp
-
2,4-dienoyl-coa
- gluteus
-
glyoxysomes
-
schulz
-
hydroxyacyl-coas
- trans-2-enoyl-coa
- biofuel production
- pharmacology
- medicine
- synthesis
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
(S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase, (S)-3-hydroxybutyryl-CoA dehydrogenase, (S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase, 1-specific DPN-linked beta-hydroxybutyric dehydrogenase, 17beta-HSD10, 3-HADH, 3-hydroxyacetyl-coenzyme A dehydrogenase, 3-hydroxyacyl coenzyme A dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase II, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase
(S)-3-hydroxybutyryl-CoA dehydrogenase
(S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase
1-specific DPN-linked beta-hydroxybutyric dehydrogenase
-
-
-
-
3-HADH
3-hydroxyacetyl-coenzyme A dehydrogenase
-
-
-
-
3-hydroxyacyl coenzyme A dehydrogenase
-
-
-
-
3-hydroxyacyl-CoA dehydrogenase
3-hydroxyacyl-coenzyme A dehydrogenase
3-hydroxyadipyl-CoA dehydrogenase
3-hydroxyadipyl-CoA dehydrogenase (NAD+) (probably (S)-3-specific)
3-hydroxyisobutyryl-CoA dehydrogenase
-
-
-
-
3-keto reductase
-
-
-
-
3-L-hydroxyacyl-CoA dehydrogenase
-
-
-
-
3-L-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
3beta-hydroxyacyl coenzyme A dehydrogenase
-
-
-
-
beta hydroxyacyl dehydrogenase
-
-
-
-
beta-hydroxy acid dehydrogenase
-
-
-
-
beta-hydroxyacyl CoA dehydrogenase
-
-
-
-
beta-hydroxyacyl-coenzyme A synthetase
-
-
-
-
beta-hydroxybutyrylcoenzyme A dehydrogenase
-
-
-
-
beta-keto-reductase
-
-
-
-
beta-ketoacyl-CoA reductase
betahydroxyacylcoenzyme A dehydrogenase
-
-
-
-
endoplasmic reticulum-associated amyloid beta-peptide binding protein
-
-
-
-
FadB'
FadB2
Ferp_1035
Fum13p
H16_A0461
HAD
HADH
HADHSC
HCDH
-
-
-
-
L-3-hydroxyacyl CoA dehydrogenase
-
-
-
-
L-3-hydroxyacyl-CoA dehydrogenase
L-3-hydroxyacyl-CoA dehydrogenase, short chain
L-3-hydroxyacylcoenzyme A dehydrogenase
-
-
-
-
LIC13300
Msed_0399
multifunctional beta-oxidation enzyme
PaaH
PaaH1
RePaaH1
SCHAD
Scully protein
-
-
-
-
short chain L-3-hydroxyacyl-CoA dehydrogenase
-
displays optimal activity using 6-carbon substrates
short-chain 3-hydroxyacyl-CoA dehydrogenase
short-chain L-3-hydroxyacyl-CoA dehydrogenase
TFP
-
trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3
type II HADH
-
-
-
-
additional information
(S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase
-
(S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase
-
-
beta-ketoacyl-CoA reductase
-
-
-
-
Ferp_1035
gene name. Bifunctional crotonase/3-OH-butyryl-CoA dehydrogenase
Ferp_1035
gene name. Bifunctional crotonase/3-OH-butyryl-CoA dehydrogenase
-
Msed_0399
locus name, bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
Msed_0399
locus name, bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
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additional information
-
PaaH is a member of the alcohol dehydrogenase family
additional information
-
PaaH is a member of the alcohol dehydrogenase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
-
-
-
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
highly conserved residue Ser137 is essential for activity
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
molecular reaction mechanism, a His-Glu pair is essential for actalysis in the active site
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
reaction mechanism via enolate intermediate
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
structure-function analysis and catalytic mechanism, overview
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
structure-function analysis using the crystal structure, PDB ID 4j0f, and catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Benzoate degradation, Biosynthesis of secondary metabolites, Butanoate metabolism, Caprolactam degradation, Carbon fixation pathways in prokaryotes, Fatty acid degradation, Fatty acid elongation, Geraniol degradation, Lysine degradation, Microbial metabolism in diverse environments, Toluene degradation, Tryptophan metabolism, Valine, leucine and isoleucine degradation
MetaCyc
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered), 2-methyl-branched fatty acid beta-oxidation, 2-methylpropene degradation, 3-hydroxypropanoate/4-hydroxybutanate cycle, 4-hydroxybenzoate biosynthesis III (plants), androstenedione degradation I (aerobic), androstenedione degradation II (anaerobic), benzoyl-CoA degradation I (aerobic), cholesterol degradation to androstenedione I (cholesterol oxidase), cholesterol degradation to androstenedione II (cholesterol dehydrogenase), crotonate fermentation (to acetate and cyclohexane carboxylate), fatty acid beta-oxidation I (generic), fatty acid beta-oxidation II (plant peroxisome), fatty acid beta-oxidation VI (mammalian peroxisome), fatty acid salvage, glutaryl-CoA degradation, L-glutamate degradation V (via hydroxyglutarate), methyl ketone biosynthesis (engineered), methyl tert-butyl ether degradation, oleate beta-oxidation, phenylacetate degradation I (aerobic), platensimycin biosynthesis, pyruvate fermentation to butanoate, pyruvate fermentation to butanol I, pyruvate fermentation to butanol II (engineered), pyruvate fermentation to hexanol (engineered), valproate beta-oxidation
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SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
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CAS REGISTRY NUMBER
COMMENTARY
9028-40-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
cf. EC 1.1.1.36
-
-
r
1-propanol + NAD+
n-propanal + NADH
-
multifunctional enzyme from brain
-
ir
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-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-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
-
key enzyme involved in fatty acid oxidation
-
-
r
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-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-beta-alanylcysteamine + NADH
(S)-3-hydroxybutyryl-N-beta-alanylcysteamine + NAD+
-
-
-
r
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
(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+
-
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+
-
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+
enzyme FadB' converts (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA, while no conversion of (R)-3-hydroxybutyryl-CoA is detected
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-
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
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-
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
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-
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
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-
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
-
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
-
highest activity with acetoacetyl-CoA, significant activity with increasing chain length up to C16
-
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-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
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
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-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
-
-
?
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-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
-
-
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
17beta-estradiol + NAD+
estrone + NADH
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
-
-
-
-
?
3-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
-
key enzyme involved in fatty acid oxidation
-
-
r
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
-
inactivation
-
-
?
(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+
-
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+
-
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+
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
-
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
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-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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme prefers NAD+. NADP(H) is utilized at a rate of less than 10% in comparison to activity with NAD(H)
-
NAD+
-
-
NAD+
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
NAD+
mode of cofactor binding, overview. The NAD+-binding site is located at the G-x-G-x-x-G nucleotide-binding motif, comprising residues Gly8-Ala9-Gly10-Thr11-Met12-Gly13. The hydroxyl groups of a phosphate moiety are hydrogen-bonded with the main chain nitrogen atoms of Thr11 and Met12. The nicotinamide and the two ribose rings of NAD+ are stabilized through hydrogen bond interactions mediated by the conserved Asp31, Glu90, Lys95, Asn115, Ser117, and Asn141 residues. The adenine moiety of NAD+ is positioned at the hydrophobic pocket formed by hydrophobic residues such as Leu7, Ile32, Ala88, Ile89, Ile94, and Ile98. One exception is Arg30, which assists the binding of the adenine moiety of NAD+ through a hydrogen bond
NAD+
the NAD+ cofactor is bound to the N-terminal Rossmann fold, the NAD+-binding pocket is made up of 5 loops, enzyme binding structure analysis, overview
NADH
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA
NADPH
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
inhibits the enzyme by 50% at 0.1 mM, further increase of inhibitor concentration reduces the activity of FadB' drastically
CoA
inhibits the enzyme by 20% at 0.1 mM, further increase of inhibitor concentration reduces the activity of FadB' drastically
EDTA
about 35% inhibition at 1 mM, about 25% inhibition at 10 mM
K+
about 30% inhibition at 1 mM, about 20% inhibition at 10 mM
RNAi
-
suppressed KCR activity results in a reduction of cuticular wax load and affects very-long-chain fatty acid composition of sphingolipids, seed triacylglycerols, and root glycerolipids
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.088
(S)-3-hydroxydecanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxydecanoyl-CoA
0.0505
(R)-3-hydroxyacyl-CoA
recombinant mutant Y209A, pH 7.0, 25ĆĀ°C
0.0721
(R)-3-hydroxyacyl-CoA
recombinant wild-type enzyme, pH 7.0, 25ĆĀ°C
0.0833
(R)-3-hydroxyacyl-CoA
recombinant mutant R204A, pH 7.0, 25ĆĀ°C
0.1157
(R)-3-hydroxyacyl-CoA
recombinant mutant R204A/Y209A, pH 7.0, 25ĆĀ°C
0.0699
(S)-3-hydroxybutyryl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxybutyryl-CoA
0.0286
(S)-3-hydroxyhexanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxyhexanoyl-CoA
0.0163
(S)-3-hydroxyoctanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxyoctanoyl-CoA
0.0096
3-acetoacetyl-CoA
-
mutant enzyme H138A, at pH 7.5 and 37ĆĀ°C
0.0227
3-acetoacetyl-CoA
-
wild type enzyme, at pH 7.5 and 37ĆĀ°C
0.076
acetoacetyl-CoA
pH 6.5, 30ĆĀ°C, recombinant enzyme in presence of 0.1 mM acetyl-CoA
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 8
(R)-3-hydroxyacyl-CoA
recombinant mutant R204A, pH 7.0, 25ĆĀ°C
10
(R)-3-hydroxyacyl-CoA
recombinant mutant R204A/Y209A, pH 7.0, 25ĆĀ°C
17
(R)-3-hydroxyacyl-CoA
recombinant mutant Y209A, pH 7.0, 25ĆĀ°C
45
(R)-3-hydroxyacyl-CoA
recombinant wild-type enzyme, pH 7.0, 25ĆĀ°C
104.3
3-acetoacetyl-CoA
-
mutant enzyme H138A, at pH 7.5 and 37ĆĀ°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
90
(R)-3-hydroxyacyl-CoA
recombinant mutant R204A/Y209A, pH 7.0, 25ĆĀ°C
300
(R)-3-hydroxyacyl-CoA
recombinant mutants R204A and Y209A, pH 7.0, 25ĆĀ°C
600
(R)-3-hydroxyacyl-CoA
recombinant wild-type enzyme, pH 7.0, 25ĆĀ°C
0.011
3-acetoacetyl-CoA
-
mutant enzyme H138A, at pH 7.5 and 37ĆĀ°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.48
-
enzyme activity in inner membrane of liver mitochondria, substrate acetoacetyl-CoA
0.75
-
72% activivty is bound to the matrix surface of the inner mitochondria membrane, binding is inhibited by increasing ionic strength and pH
1.5
16.5
purified recombinant enzyme, pH 6.5, 30ĆĀ°C, substrate (S)-3-hydroxybutanoyl-CoA with NAD+
23.4
-
L-3-hydroxyacyl-CoA dehydrogenase activity of the trifunctional beta-oxidation protein
3 - 8
pH 8.0, 65ĆĀ°C, native enzyme, autotrophically- or heterotrophically-grown cell
3.4
-
enzyme activity in matrix of liver mitochondria, substrate acetoacetyl-CoA
4.17
-
(S)-3-hydroxydecanoyl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
4.22
-
(S)-3-hydroxybutyryl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
additional information
-
the N-terminal His-tag does notinfluence enzyme activity
1.5
purified recombinant enzyme, pH 6.5, 30ĆĀ°C, substrate (S)-3-hydroxybutanoyl-CoA with NADP+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
5.5 - 6.5
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA decreases above pH 6.5
6 - 7
9.6
10
NAD+-dependent dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
maximal activity at pH 6.0-7.0, 65% and 75% activity at pH 5.0 and pH 8.0, respectively, and 46% of the maximal activity at pH 10.0, and 26% of maximal activity at pH 4.0
9 - 11
pH 9.0: about 45% of maximal activity, pH 11.0: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
37
NAD+-dependent dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
multifunctional beta-oxidation enzyme complex composed of 2 different 3-hydroyacyl-CoA dehydrogenases, 2 different 2-enoyl-CoA hydratases, thiolase, and epimerase activities
-
-
brenda
multifunctional beta-oxidation enzyme complex composed of 2 different 3-hydroyacyl-CoA dehydrogenases, 2 different 2-enoyl-CoA hydratases, thiolase, and epimerase activities
-
-
brenda
-
33713, 286590, 286593, 286594, 286596, 286598, 286606, 286607, 286608, 286609, 286610, 286611, 673530
-
-
brenda
isozyme 3-ketoacyl-CoA reductase 1; high erucic acid rapeseed variant, two isozymes encoded by genes Bn-kcr1 and Bn-kcr2, two cultivars Gaspard and ISLR4
SwissProt
brenda
isozyme 3-ketoacyl-CoA reductase 2; high erucic acid rapeseed variant, two isozymes encoded by genes Bn-kcr1 and Bn-kcr2, two cultivars Gaspard and ISLR4
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
activity of the enzyme it encodes is particularly high in the pancreas and especially in the islets of Langerhans
brenda
-
in oocytes from diabetic mice, activity of Hadh2 is significantly reduced
brenda
-
high level expression in malignant prostatic epithelial cells
brenda
additional information
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
brenda
-
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
-
brenda
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
brenda
-
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
-
brenda
-
-
brenda
-
immunohistochemic analysis, more intense staining in islets than in the surrounding exocrine tissue, being strongly present in insulin-positive cells and only weakly in glucagon-positive alpha cells
brenda
high HADH expression level, activity of the enzyme it encodes is particularly high in the pancreas and especially in the islets of Langerhans
brenda
additional information
-
KCR1 and KCR2 transcripts in inflorescence stems
brenda
additional information
enzyme detection in urine of infected Mesocricetus auratus: leptospiral protein, 3-hydroxyacyl-CoA dehydrogenase (HADH), is found to be excreted in the urine of hamsters during the early phase of infection
brenda
additional information
-
enzyme detection in urine of infected Mesocricetus auratus: leptospiral protein, 3-hydroxyacyl-CoA dehydrogenase (HADH), is found to be excreted in the urine of hamsters during the early phase of infection
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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
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 specifically catalyzes the third step of beta oxidation
-
metabolism
-
the enzyme is involved in fatty acid degradation metabolism
-
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)-3Ć¢ĀĀspecific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
physiological function
-
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
-
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
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
-
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)-3Ć¢ĀĀspecific] 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
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM