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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 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.157 3-hydroxybutyryl-CoA dehydrogenase
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 1.1.1.157
- clostridium
- crotonase
-
thiolase
- acetoacetyl-coa
-
s-3-hydroxybutyryl-coa
- acetobutylicum
- n-butanol
- eutropha
- crotonyl-coa
- butyricum
- beijerinckii
- kluyveri
- beta-ketothiolase
showSynonyms
3-hydroxybutyryl-coa dehydrogenase, beta-hydroxybutyryl-coa dehydrogenase, (s)-3-hydroxybutyryl-coa dehydrogenase, cp 26, beta-hydroxybutyryl coenzyme a dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-3-hydroxybutyryl-CoA dehydrogenase
beta-hydroxybutyryl coenzyme A dehydrogenase
-
-
-
-
beta-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
BHB
BHBD
-
-
-
-
CP 26
-
-
-
-
CP26
DebiaDRAFT_04571
dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
HBD
L(+)-3-hydroxybutyryl-CoA dehydrogenase
L-(+)-3-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
Msed_0399
DebiaDRAFT_04571
Desulfococcus biacutus KMRActS (DSM 5651)
-
-
-
DebiaDRAFT_04571
Desulfococcus biacutus KMRActS DSM 5651
-
-
-
L(+)-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
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
-
Substrates: -
Products: -
Products: -
r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS (DSM 5651)
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS DSM 5651
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
Alkalihalophilus marmarensis GMBE 72T
-
Substrates: -
Products: -
Products: -
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: synthesis of butyrate
Products: -
Products: -
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: NADPH-dependent enzyme specific for 3-hydroxybutyryl-CoA
Products: -
Products: -
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: 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
Products: -
Products: -
r
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
-
Substrates: -
Products: -
Products: -
?
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reaction is observed with NADP+
Products: -
Products: -
?
additional information
?
-
Desulfococcus biacutus KMRActS (DSM 5651)
-
Substrates: no reaction is observed with NADP+
Products: -
Products: -
?
additional information
?
-
Desulfococcus biacutus KMRActS DSM 5651
-
Substrates: no reaction is observed with NADP+
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
?
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
-
Substrates: -
Products: -
Products: -
r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS (DSM 5651)
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS DSM 5651
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
Alkalihalophilus marmarensis GMBE 72T
-
Substrates: -
Products: -
Products: -
?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: -
Products: -
Products: -
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
-
Substrates: synthesis of butyrate
Products: -
Products: -
?
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
-
Substrates: -
Products: -
Products: -
?
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Confusion
Species-related differences in the electrophoretic behavior of CP 29 and CP 26: An immunochemical analysis.
Tuberculosis
Characterization of a {beta}-hydroxybutyryl-CoA dehydrogenase from Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0096
3-acetoacetyl-CoA
-
mutant enzyme H138A, at pH 7.5 and 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.1
-
reduction of 250 mM acetoacetyl-CoA in the presence of 0.5 mM NADH, at pH 8.0 and 30°C
23.3
-
oxidation of 0.05 mM 3-hydroxybutyryl-CoA in the presence of 5 mM NAD+, at pH 8.0 and 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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
-
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
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
an increase in the NADPH level and the activity of 3-hydroxybutyryl-CoA dehydrogenase can increase the accumulation of polyhydroxybutyrate in the cells of Bacillus marmarensis
metabolism
Alkalihalophilus marmarensis GMBE 72T
-
an increase in the NADPH level and the activity of 3-hydroxybutyryl-CoA dehydrogenase can increase the accumulation of polyhydroxybutyrate in the cells of Bacillus marmarensis
-
Show AA Sequence and Transmembrane Helices (116 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Desulfococcus biacutus KMRActS (DSM 5651)
-
x * 28000, calculated from amino acid sequence
-
?
Desulfococcus biacutus KMRActS (DSM 5651)
-
x * 31000, His6-tagged enzyme, SDS-PAGE
-
?
Desulfococcus biacutus KMRActS DSM 5651
-
x * 28000, calculated from amino acid sequence
-
?
Desulfococcus biacutus KMRActS DSM 5651
-
x * 31000, His6-tagged enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo and NAD+-bound enzyme forms, hanging drop vapor diffusion method. NAD+-bound crystals grow using a reservoir solution consisting of 17.5% (w/v) PEG 3350, 200 mM sodium thiocyanate. Apo crystals grow using a reservoir solution consisting of 1.25% (w/v) PEG 400, 2.2 M ammonium sulfate, 0.1 M HEPES-NaOH pH 7.5
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H138A
-
the mutant shows a slightly lower Km value and a significantly lower kcat value than the wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni cOmplete column chromatography and Mono Q column chromatography
-
simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Clostridium coskatii and Clostridium ljungdahlii
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is strongly induced in acetone-grown cells
the enzyme expression is strongly induced in acetone-grown cells
Desulfococcus biacutus KMRActS DSM 5651
-
-
the enzyme expression is strongly induced in acetone-grown cells
Desulfococcus biacutus KMRActS (DSM 5651)
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Fluechter, S.; Follonier, S.; Schiel-Bengelsdorf, B.; Bengelsdorf, F.R.; Zinn, M.
Anaerobic production of poly(3-hydroxybutyrate) and its precursor 3?hydroxybutyrate from synthesis gas by autotrophic clostridia
Biomacromolecules
20
3271-3282
2019
Clostridium scatologenes (A0A0E3GR61)
brenda
Takenoya, M.; Taguchi, S.; Yajima, S.
Crystal structure and kinetic analyses of a hexameric form of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium acetobutylicum
Acta Crystallogr. Sect. F
74
733-740
2018
Clostridium acetobutylicum
brenda
Frey, J.; Schneider, F.; Huhn, T.; Spiteller, D.; Schink, B.; Schleheck, D.
Two enzymes of the acetone degradation pathway of Desulfococcus biacutus coenzyme B12-dependent 2-hydroxyisobutyryl-CoA mutase and 3-hydroxybutyryl-CoA dehydrogenase
Environ. Microbiol. Rep.
10
283-292
2018
Desulfococcus biacutus, Desulfococcus biacutus KMRActS DSM 5651, Desulfococcus biacutus KMRActS (DSM 5651)
brenda
Atakav, Y.; Pinar, O.; Kazan, D.
Investigation of the physiology of the obligate alkaliphilic Bacillus marmarensis GMBE 72T considering its alkaline adaptation mechanism for poly(3-hydroxybutyrate) synthesis
Microorganisms
9
462
2021
Alkalihalophilus marmarensis, Alkalihalophilus marmarensis GMBE 72T
brenda
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