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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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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
beta-hydroxybutyryl-coa dehydrogenase, cp 26, (s)-3-hydroxybutyryl-coa dehydrogenase, beta-hydroxybutyryl coenzyme a dehydrogenase,
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(S)-3-hydroxybutyryl-CoA dehydrogenase
beta-hydroxybutyryl coenzyme A dehydrogenase
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beta-hydroxybutyryl-CoA dehydrogenase
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dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate)
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L(+)-3-hydroxybutyryl-CoA dehydrogenase
L-(+)-3-hydroxybutyryl-CoA dehydrogenase
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(S)-3-hydroxybutyryl-CoA dehydrogenase
A4YDS4
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(S)-3-hydroxybutyryl-CoA dehydrogenase
A4YDS4
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L(+)-3-hydroxybutyryl-CoA dehydrogenase
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L(+)-3-hydroxybutyryl-CoA dehydrogenase
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Msed_0399
A4YDS4
locus name
Msed_0399
A4YDS4
locus name
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(S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
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(S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
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3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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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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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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3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
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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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NADPH
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specific for NADPH
NADPH
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the rate with NADH is below 0.25% of that with NADPH
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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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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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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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445
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reduction of 3-acetoacetyl-CoA, pH 6.5, 25°C
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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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assay at
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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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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7.8
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isoelectric focusing, pH 3.5-10.0
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brenda
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A4YDS4
UniProt
brenda
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A4YDS4
UniProt
brenda
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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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Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
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26000
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8 * 26000, SDS-PAGE
33500
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x * 33500, SDS-PAGE
220000
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equilibrium sedimentation
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octamer
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8 * 26000, SDS-PAGE
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simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase
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Hartmanis, M.G.N.; Sliwkowski, M.X.
Selenomethionine-containing thiolase and 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri
Curr. Top. Cell. Regul.
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479-486
1985
Clostridium kluyveri
brenda
Sliwkowski, M.X.; Hartmanis, M.G.N.
Simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri
Anal. Biochem.
141
344-347
1984
Clostridium kluyveri
brenda
Madan, V.K.; Hillmer, P.; Gottschalk, G.
Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri
Eur. J. Biochem.
32
51-56
1973
Clostridium kluyveri
brenda
Hawkins, A.B.; Adams, M.W.; Kelly, R.M.
Conversion of 4-hydroxybutyrate to acetyl coenzyme A and its anapleurosis in the Metallosphaera sedula 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
Appl. Environ. Microbiol.
80
2536-2545
2014
Metallosphaera sedula (A4YDS4), Metallosphaera sedula DSM 5348 (A4YDS4)
brenda
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