Information on EC 1.1.1.157 - 3-hydroxybutyryl-CoA dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.157
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RECOMMENDED NAME
GeneOntology No.
3-hydroxybutyryl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
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butanoate fermentation
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Butanoate metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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Phenylalanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
39319-78-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
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
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenium
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the enzyme contains selenomethionine. Incorporation of selenium into the enzyme occurs randomly and is not required for any specific function
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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0.05 mM, 80% inhibition
iodoacetamide
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1 mM, slight inhibition
N-ethylmaleimide
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1 mM, slight inhibition
p-chloromercuribenzoate
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1 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
3-acetoacetyl-CoA
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pH 6.5, 25C
0.07
NADPH
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pH 6.5, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
292
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pH 6.5, 25C
445
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reduction of 3-acetoacetyl-CoA, pH 6.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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at the pH optimum 6.5 the reduction of 3-acetoacetyl-CoA is 14times faster than the oxidation of (S)-3-hydroxybutanoyl-CoA at its pH optimum 9.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
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pH 5: about 35% of maximal activity, pH 7.5: about 55% of maximal activity, reduction of 3-acetoacetyl-CoA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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isoelectric focusing, pH 3.5-10.0
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
215000
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gel filtration
220000
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equilibrium sedimentation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 33500, SDS-PAGE
octamer
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8 * 26000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase
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