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Enzyme Nomenclature
Information on EC 1.1.1.157 - 3-hydroxybutyryl-CoA dehydrogenase
for references in articles please use BRENDA:EC1.1.1.157
Word Map on EC 1.1.1.157
- 1.1.1.157
- clostridium
- acetyl-coa
- crotonase
-
thiolase
- acetoacetyl-coa
- acetobutylicum
- n-butanol
- cr
-
s-3-hydroxybutyryl-coa
- eutropha
- butyricum
- beta-ketothiolase
- kluyveri
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.157
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RECOMMENDED NAME
GeneOntology No.
3-hydroxybutyryl-CoA dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
39319-78-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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null mutant 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
physiological function
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null mutant 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
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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
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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-
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?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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-
-
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r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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synthesis of butyrate
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-
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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NADPH-dependent enzyme specific for 3-hydroxybutyryl-CoA
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r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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the oxidation of (S)-3-hydroxybutanoyl-CoA at pH 9.5 proceeds with 7% of the rate of the 3-acetoacetyl-CoA reduction. At pH 6.5, the reduction of 3-acetoacetyl-CoA is 14times faster than the oxidation of (S)-3-hydroxybutanoyl-CoA.The enzyme does not oxidize 3-hydroxyvaleryl-CoA or 3-hydroxycaproyl-CoA
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r
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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-
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r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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synthesis of butyrate
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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
6.5
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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
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
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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)
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