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
1.1.1.157
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxybutyryl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
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
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
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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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SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(S)-3-hydroxybutyryl-CoA dehydrogenase
A4YDS4
-
(S)-3-hydroxybutyryl-CoA dehydrogenase
A4YDS4
-
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beta-hydroxybutyryl coenzyme A dehydrogenase
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-
-
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beta-hydroxybutyryl-CoA dehydrogenase
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-
-
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BHBD
-
-
-
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CP 26
-
-
-
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dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate)
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-
-
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L(+)-3-hydroxybutyryl-CoA dehydrogenase
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-
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L(+)-3-hydroxybutyryl-CoA dehydrogenase
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L-(+)-3-hydroxybutyryl-CoA dehydrogenase
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-
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Msed_0399
A4YDS4
locus name
Msed_0399
A4YDS4
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
39319-78-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
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
Mycobacterium tuberculosis ATCC 25618
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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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
-
synthesis of butyrate
-
-
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
-
NADPH-dependent enzyme specific for 3-hydroxybutyryl-CoA
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-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
-
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
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
show the reaction diagram
-
synthesis of butyrate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
specific for NADPH
NADPH
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the rate with NADH is below 0.25% of that with NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
selenium
-
the enzyme contains selenomethionine. Incorporation of selenium into the enzyme occurs randomly and is not required for any specific function
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.05 mM, 80% inhibition
iodoacetamide
-
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
LITERATURE
IMAGE
0.05
3-acetoacetyl-CoA
-
pH 6.5, 25C
0.07
NADPH
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pH 6.5, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
292
-
pH 6.5, 25C
445
-
reduction of 3-acetoacetyl-CoA, pH 6.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
LITERATURE
5 - 7.5
-
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
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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isoelectric focusing, pH 3.5-10.0
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
215000
-
gel filtration
286053
220000
-
equilibrium sedimentation
286053
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 33500, SDS-PAGE
octamer
-
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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