Information on EC 1.1.1.157 - 3-hydroxybutyryl-CoA dehydrogenase

for references in articles please use BRENDA:EC1.1.1.157
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The expected taxonomic range for this enzyme is: Bacteria, Archaea

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EC NUMBER
COMMENTARY hide
1.1.1.157
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RECOMMENDED NAME
GeneOntology No.
3-hydroxybutyryl-CoA dehydrogenase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
butanoate fermentation
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Phenylalanine metabolism
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Benzoate degradation
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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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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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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
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
3-acetoacetyl-CoA
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pH 6.5, 25°C
0.07
NADPH
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pH 6.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
292
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pH 6.5, 25°C
445
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reduction of 3-acetoacetyl-CoA, pH 6.5, 25°C
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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
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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isoelectric focusing, pH 3.5-10.0
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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8 * 26000, SDS-PAGE
33500
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x * 33500, SDS-PAGE
215000
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gel filtration
220000
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equilibrium sedimentation
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 33500, SDS-PAGE
octamer
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8 * 26000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.157)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)