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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
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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(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
Alkalihalophilus marmarensis
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(S)-3-hydroxybutyryl-CoA dehydrogenase
Alkalihalophilus marmarensis GMBE 72T
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(S)-3-hydroxybutyryl-CoA dehydrogenase
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(S)-3-hydroxybutyryl-CoA dehydrogenase
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(S)-3-hydroxybutyryl-CoA dehydrogenase
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BHB
Alkalihalophilus marmarensis
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BHB
Alkalihalophilus marmarensis GMBE 72T
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CP26
Alkalihalophilus marmarensis
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CP26
Alkalihalophilus marmarensis GMBE 72T
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DebiaDRAFT_04571
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DebiaDRAFT_04571
Desulfococcus biacutus KMRActS (DSM 5651)
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DebiaDRAFT_04571
Desulfococcus biacutus KMRActS DSM 5651
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HBD
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L(+)-3-hydroxybutyryl-CoA dehydrogenase
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L(+)-3-hydroxybutyryl-CoA dehydrogenase
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Msed_0399
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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(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
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?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
additional information
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(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
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r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
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r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
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r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
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r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS (DSM 5651)
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r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS DSM 5651
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r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
Alkalihalophilus marmarensis
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3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
Alkalihalophilus marmarensis GMBE 72T
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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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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
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
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3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
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3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
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additional information
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no reaction is observed with NADP+
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additional information
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Desulfococcus biacutus KMRActS (DSM 5651)
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no reaction is observed with NADP+
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additional information
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Desulfococcus biacutus KMRActS DSM 5651
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no reaction is observed with NADP+
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(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
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?
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
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r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
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r
(S)-3-hydroxybutanoyl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
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r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
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r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS (DSM 5651)
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3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutanoyl-CoA + NAD+
Desulfococcus biacutus KMRActS DSM 5651
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3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
Alkalihalophilus marmarensis
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3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutanoyl-CoA + NADP+
Alkalihalophilus marmarensis GMBE 72T
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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-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
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3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS (DSM 5651)
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3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
Desulfococcus biacutus KMRActS DSM 5651
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NAD+
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NADP+
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NADPH
Alkalihalophilus marmarensis
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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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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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0.0096 - 0.05
3-acetoacetyl-CoA
0.07
NADPH
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pH 6.5, 25°C
0.0096
3-acetoacetyl-CoA
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mutant enzyme H138A, at pH 7.5 and 37°C
0.0227
3-acetoacetyl-CoA
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wild type enzyme, at pH 7.5 and 37°C
0.05
3-acetoacetyl-CoA
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pH 6.5, 25°C
0.0168
NADH
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mutant enzyme H138A, at pH 7.5 and 37°C
0.0314
NADH
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wild type enzyme, at pH 7.5 and 37°C
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104.3 - 13000
3-acetoacetyl-CoA
104.3
3-acetoacetyl-CoA
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mutant enzyme H138A, at pH 7.5 and 37°C
13000
3-acetoacetyl-CoA
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wild type enzyme, at pH 7.5 and 37°C
93.8
NADH
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mutant enzyme H138A, at pH 7.5 and 37°C
8500
NADH
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wild type enzyme, at pH 7.5 and 37°C
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11000 - 630000
3-acetoacetyl-CoA
11000
3-acetoacetyl-CoA
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mutant enzyme H138A, at pH 7.5 and 37°C
630000
3-acetoacetyl-CoA
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wild type enzyme, at pH 7.5 and 37°C
5600
NADH
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mutant enzyme H138A, at pH 7.5 and 37°C
270000
NADH
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wild type enzyme, at pH 7.5 and 37°C
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14.1
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reduction of 250 mM acetoacetyl-CoA in the presence of 0.5 mM NADH, at pH 8.0 and 30°C
23.3
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oxidation of 0.05 mM 3-hydroxybutyryl-CoA in the presence of 5 mM NAD+, at pH 8.0 and 30°C
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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Alkalihalophilus marmarensis
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brenda
Alkalihalophilus marmarensis GMBE 72T
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brenda
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brenda
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brenda
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UniProt
brenda
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brenda
Desulfococcus biacutus KMRActS (DSM 5651)
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brenda
Desulfococcus biacutus KMRActS DSM 5651
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brenda
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UniProt
brenda
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UniProt
brenda
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brenda
Desulfococcus biacutus KMRActS (DSM 5651)
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brenda
Desulfococcus biacutus KMRActS DSM 5651
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brenda
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metabolism
Alkalihalophilus marmarensis
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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
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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
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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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220000
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equilibrium sedimentation
26000
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8 * 26000, SDS-PAGE
33500
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x * 33500, SDS-PAGE
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octamer
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8 * 26000, SDS-PAGE
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x * 33500, SDS-PAGE
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x * 28000, calculated from amino acid sequence
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x * 31000, His6-tagged enzyme, SDS-PAGE
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Desulfococcus biacutus KMRActS (DSM 5651)
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x * 28000, calculated from amino acid sequence
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Desulfococcus biacutus KMRActS (DSM 5651)
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x * 31000, His6-tagged enzyme, SDS-PAGE
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Desulfococcus biacutus KMRActS DSM 5651
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x * 28000, calculated from amino acid sequence
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?
Desulfococcus biacutus KMRActS DSM 5651
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x * 31000, His6-tagged enzyme, SDS-PAGE
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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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H138A
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the mutant shows a slightly lower Km value and a significantly lower kcat value than the wild type enzyme
N188A
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the mutant abolishes the enzyme activity
S117A
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the mutant abolishes the enzyme activity
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Ni cOmplete column chromatography and Mono Q column chromatography
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Ni-NTA column chromatography
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Ni-NTA column chromatography, and Superdex 200 gel filtration
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simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase
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expressed in Clostridium coskatii and Clostridium ljungdahlii
expressed in Escherichia coli Rosetta 2 cells
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expressed in Escherichia coli Rosetta 2(DE3) cells
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the enzyme expression is strongly induced in acetone-grown cells
the enzyme expression is strongly induced in acetone-grown cells
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the enzyme expression is strongly induced in acetone-grown cells
Desulfococcus biacutus KMRActS (DSM 5651)
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the enzyme expression is strongly induced in acetone-grown cells
Desulfococcus biacutus KMRActS DSM 5651
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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
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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