Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase and Organism(s) Homo sapiens

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Homo sapiens


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
1.1.1.35
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxyacyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
show the reaction diagram
structure-function analysis and catalytic mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered)
-
-
2-methylpropene degradation
-
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3-hydroxypropanoate/4-hydroxybutanate cycle
-
-
4-hydroxybenzoate biosynthesis V
-
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androstenedione degradation
-
-
benzoyl-CoA degradation I (aerobic)
-
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cholesterol degradation to androstenedione I (cholesterol oxidase)
-
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cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
-
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crotonate fermentation (to acetate and cyclohexane carboxylate)
-
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fatty acid beta-oxidation I
-
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fatty acid beta-oxidation II (peroxisome)
-
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fatty acid beta-oxidation VI (peroxisome)
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fatty acid salvage
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glutaryl-CoA degradation
-
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jasmonic acid biosynthesis
-
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L-glutamate degradation V (via hydroxyglutarate)
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methyl ketone biosynthesis (engineered)
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methyl tert-butyl ether degradation
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phenylacetate degradation I (aerobic)
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pyruvate fermentation to butanoate
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pyruvate fermentation to butanol I
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pyruvate fermentation to butanol II (engineered)
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pyruvate fermentation to hexanol (engineered)
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toluene degradation to benzoyl-CoA (anaerobic)
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adipate degradation
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butanoate fermentation
-
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CO2 fixation in Crenarchaeota
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lipid metabolism
-
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phenylacetate degradation (aerobic)
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tryptophan metabolism
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Fatty acid elongation
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Fatty acid degradation
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Primary bile acid biosynthesis
-
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Valine, leucine and isoleucine degradation
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Geraniol degradation
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Lysine degradation
-
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Benzoate degradation
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Tryptophan metabolism
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Toluene degradation
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Butanoate metabolism
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Carbon fixation pathways in prokaryotes
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Caprolactam degradation
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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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]).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-40-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
Caenorhabditis elegans HAD is highly conserved to human HAD
malfunction
metabolism
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3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation
physiological function
-
important role for HADH in insulin secretion
additional information
-
molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects, molecular dynamics simulation, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
1-propanol + NAD+
n-propanal + NADH
show the reaction diagram
-
multifunctional enzyme from brain
-
ir
17beta-estradiol + NAD+
estrone + NADH
show the reaction diagram
17beta-estradiol + NAD+
estrone + NADH + H+
show the reaction diagram
2-propanol + NAD+
acetone + NADH
show the reaction diagram
-
multifunctional enzyme from brain
-
ir
3-ketohexadecanoyl-CoA + NADH
(S)-3-hydroxhexadecanoyl-CoA + NAD+
show the reaction diagram
-
-
r
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
-
-
r
3-oxohexadecanoyl-CoA + NADH + H+
(S)-3-hydroxhexadecanoyl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
3-oxooctanoyl-CoA + NADH + H+
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
show the reaction diagram
5alpha-dihydrotestosterone + NADH
(3beta,5alpha,17beta)-androstane-3,17-diol + NAD+
show the reaction diagram
-
-
-
r
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
allopregnanolone + NAD+
5alpha-dihydroprogesterone + NADH
show the reaction diagram
androsterone + NAD+
androstanedione + NADH
show the reaction diagram
-
-
-
ir
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
17beta-estradiol + NAD+
estrone + NADH
show the reaction diagram
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH + H+
show the reaction diagram
-
inactivation
-
-
?
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
show the reaction diagram
-
inactivation
-
-
?
allopregnanolone + NAD+
5alpha-dihydroprogesterone + NADH
show the reaction diagram
-
inactivation
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034
(3beta,5alpha,17beta)-androstane-3,17-diol
-
enzyme from brain
0.000058 - 0.00529
(S)-3-hydroxybutyryl-CoA
0.043
17beta-estradiol
-
enzyme from brain
0.0138 - 0.089
acetoacetyl-CoA
0.045
androsterone
-
enzyme from brain
0.00009 - 0.242
NAD+
0.0009 - 0.0338
NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.093
(3beta,5alpha,17beta)-androstane-3,17-diol
-
enzyme from brain
375 - 1420
(S)-3-hydroxybutyryl-CoA
0.011
17beta-estradiol
-
enzyme from brain
24
3-ketohexdecanoyl-CoA
enzyme from brain, pH 7.0
28
3-ketooctanoyl-CoA
enzyme from brain, pH 7.0
21.3 - 1287
acetoacetyl-CoA
0.011
androsterone
-
enzyme from brain
705 - 1817
NAD+
176.7 - 510
NADH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
enzyme from brain, substrate 1-propanol
0.0121
-
enzyme from brain, substrate androsterone
0.0156
-
enzyme from brain, substrate 17beta-estradiol
0.087
-
enzyme from brain, substrate 5alpha-dihydrotestosterone
0.13
-
enzyme from brain, substrate dihydroandrosterone
17.35
enzyme from brain
1200
-
His-tagged recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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enzyme from brain, reduction of acetoacetyl-CoA
7
-
SCAD I and SCHAD II, pH optimum the reduction
8.5
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SCAD I, pH optimum for oxidation
9.3
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SCHAD II, pH optimum for oxidation
9.5 - 10
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enzyme from brain, oxidation of 17beta-estradiol
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activated, high level expression
Manually annotated by BRENDA team
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activity of the enzyme it encodes is particularly high in the pancreas and especially in the islets of Langerhans
Manually annotated by BRENDA team
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high level expression in malignant prostatic epithelial cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
4 * 27000, enzyme from brain, SDS-PAGE
34000
-
2 * 34000, SDS-PAGE
108000
enzyme from brain, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 34000, SDS-PAGE
homodimer
-
-
tetramer
4 * 27000, enzyme from brain, SDS-PAGE
additional information
-
structure-function relationship of SCHAD, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli, hydroxylapatite
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal hexameric histidine tag, expressed in Escherichia coli
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expressed in Escherichia coli
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gene HADHSC, located on chromosome 4q22-26
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D279E
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naturally occuring polymorphism probably involved in development of type 2 diabetes
D45G/Y214H
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a naturally occuring enzyme mutation causing human disease
H152Q
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naturally occuring polymorphism probably involved in development of type 2 diabetes
M176V
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a naturally occuring enzyme mutation causing human disease
M188V
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naturally occuring enzyme mutation, clinical data, overview
P246L
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a naturally occuring enzyme mutation causing human disease
P258L
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naturally occuring enzyme mutation, clinical data, overview
P86L
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naturally occuring polymorphism probably involved in development of type 2 diabetes
R224X
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a naturally occuring enzyme mutation causing human disease
R236X
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naturally occuring enzyme mutation, clinical data, overview
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
HADH protects against excess amino acid-induced insulin secretion
pharmacology
-
the short-chain 3-hydroxyacyl-CoA dehydrogenase is a target for intervention in case of Alzheimer's disease and Parkinson's disease