We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 1.1.1.157 - 3-hydroxybutyryl-CoA dehydrogenase for references in articles please use BRENDA:EC1.1.1.157
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
(S)-3-hydroxybutyryl-CoA dehydrogenase, beta-hydroxybutyryl coenzyme A dehydrogenase, beta-hydroxybutyryl-CoA dehydrogenase, BHBD, CP 26, dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate), L(+)-3-hydroxybutyryl-CoA dehydrogenase, L-(+)-3-hydroxybutyryl-CoA dehydrogenase, Msed_0399,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-3-hydroxybutyryl-CoA dehydrogenase
beta-hydroxybutyryl coenzyme A dehydrogenase
-
-
-
-
beta-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
L(+)-3-hydroxybutyryl-CoA dehydrogenase
L-(+)-3-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
(S)-3-hydroxybutyryl-CoA dehydrogenase
-
(S)-3-hydroxybutyryl-CoA dehydrogenase
-
-
L(+)-3-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
L(+)-3-hydroxybutyryl-CoA dehydrogenase
-
-
Msed_0399
locus name
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
-
-
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
-
-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
synthesis of butyrate
-
-
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
NADPH-dependent enzyme specific for 3-hydroxybutyryl-CoA
-
-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
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
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
-
-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
synthesis of butyrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADPH
-
specific for NADPH
NADPH
-
the rate with NADH is below 0.25% of that with NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
selenium
-
the enzyme contains selenomethionine. Incorporation of selenium into the enzyme occurs randomly and is not required for any specific function
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.05 mM, 80% inhibition
iodoacetamide
-
1 mM, slight inhibition
N-ethylmaleimide
-
1 mM, slight inhibition
p-chloromercuribenzoate
-
1 mM, complete inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.05
3-acetoacetyl-CoA
-
pH 6.5, 25°C
0.07
NADPH
-
pH 6.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
445
-
reduction of 3-acetoacetyl-CoA, pH 6.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9.5
-
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
-
assay at
6.5
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 7.5
-
pH 5: about 35% of maximal activity, pH 7.5: about 55% of maximal activity, reduction of 3-acetoacetyl-CoA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.8
-
isoelectric focusing, pH 3.5-10.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
220000
-
equilibrium sedimentation
26000
-
8 * 26000, SDS-PAGE
33500
-
x * 33500, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
octamer
-
8 * 26000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hartmanis, M.G.N.; Sliwkowski, M.X.
Selenomethionine-containing thiolase and 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri
Curr. Top. Cell. Regul.
27
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
Select items on the left to see more content.
html completed