1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase
This is an abbreviated version!
For detailed information about 3-hydroxyacyl-CoA dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.35
-
1.1.1.35
-
citrate
-
acyl-coas
-
peroxisomal
-
thiolase
-
carnitine
-
trifunctional
-
phosphofructokinase
-
hexokinase
-
endurance
-
vastus
-
lateralis
-
acetoacetyl-coa
-
medium-chain
-
soleus
-
hypoglycemia
-
extensor
-
lchad
-
acylcarnitines
-
hyperinsulinism
-
2-enoyl-coa
-
fast-twitch
-
plantaris
-
2,4-dienoyl-coa
-
schulz
-
crotonase
-
hypoketotic
-
4.1.3.7
-
glyoxysomes
-
hellp
-
3-oxoacyl-coa
-
hydroxyacyl-coas
-
trans-2-enoyl-coa
-
gluteus
-
medicine
-
biofuel production
-
diagnostics
-
pharmacology
-
synthesis
- 1.1.1.35
- citrate
- acyl-coas
- peroxisomal
-
thiolase
- carnitine
-
trifunctional
-
phosphofructokinase
- hexokinase
-
endurance
-
vastus
- lateralis
- acetoacetyl-coa
-
medium-chain
- soleus
- hypoglycemia
-
extensor
- lchad
- acylcarnitines
- hyperinsulinism
-
2-enoyl-coa
-
fast-twitch
-
plantaris
-
2,4-dienoyl-coa
-
schulz
- crotonase
-
hypoketotic
-
4.1.3.7
-
glyoxysomes
-
hellp
- 3-oxoacyl-coa
-
hydroxyacyl-coas
- trans-2-enoyl-coa
- gluteus
- medicine
- biofuel production
- diagnostics
- pharmacology
- synthesis
Reaction
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, 3-hydroxyacyl-coenzyme A dehydrogenase, 3-hydroxyadipyl-CoA dehydrogenase, 3-hydroxyadipyl-CoA dehydrogenase (NAD+) (probably (S)-3-specific), 3-hydroxybutyryl-CoA dehydrogenase, 3-hydroxyisobutyryl-CoA dehydrogenase, 3-keto reductase, 3-ketoacyl-CoA reductase, 3-L-hydroxyacyl-CoA dehydrogenase, 3-L-hydroxybutyryl-CoA dehydrogenase, 3beta-hydroxyacyl coenzyme A dehydrogenase, 3HA-CoA 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 reductase, beta-ketoacyl-CoA reductase, beta-ketoacyl-coenzyme A reductase, betahydroxyacylcoenzyme A dehydrogenase, CbHBD, endoplasmic reticulum-associated amyloid beta-peptide binding protein, F54C8.1, FadB, FadB', FadB2, Ferp_1035, Fum13p, H16_A0461, HAD, HADH, HADH2, HADHSC, HBD, HCDH, KCR1, KCR2, L-3-hydroxyacyl CoA dehydrogenase, L-3-hydroxyacyl-CoA dehydrogenase, L-3-hydroxyacyl-CoA dehydrogenase, short chain, L-3-hydroxyacylcoenzyme A dehydrogenase, L-3-hydroxybutyryl CoA dehydrogenase, L-specific 3-hydroxyacyl-CoA dehydrogenase, LIC13300, medium- and short-chain-3-hydroxyacyl-CoA dehydrogenase, medium- and short-chain-3-hydroxyacyl-coenzyme A dehydrogenase, More, Msed_0399, multifunctional beta-oxidation enzyme, NADH-3HB-CoA dehydrogenase, NADH-dependent (S)-3-hydroxyacyl-CoA dehydrogenase, NADH-dependent 3-hydroxyacyl-CoA dehydrogenase, PaaH, PaaH1, RePaaH1, SCHAD, SCHAD I, SCHAD II, SCHSD, Scully protein, short chain L-3-hydroxyacyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-coenzyme A dehydrogenase, short-chain hydroxyacyl CoA dehydrogenase, short-chain L-3-hydroxyacyl-CoA dehydrogenase, TFP, type 10 17beta-hydroxysteroid dehydrogenase, type II HADH
ECTree
1.1.1.35 3-hydroxyacyl-CoA dehydrogenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase
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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
-
-
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
-
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 + 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
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 + 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+
-
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
-
-
?
