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show all sequences of 1.1.1.157

Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri

Madan, V.K.; Hillmer, P.; Gottschalk, G.; Eur. J. Biochem. 32, 51-56 (1973)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoic acid)
0.05 mM, 80% inhibition
Clostridium kluyveri
iodoacetamide
1 mM, slight inhibition
Clostridium kluyveri
N-ethylmaleimide
1 mM, slight inhibition
Clostridium kluyveri
p-chloromercuribenzoate
1 mM, complete inhibition
Clostridium kluyveri
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.05
-
3-acetoacetyl-CoA
pH 6.5, 25°C
Clostridium kluyveri
0.07
-
NADPH
pH 6.5, 25°C
Clostridium kluyveri
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
8 * 26000, SDS-PAGE
Clostridium kluyveri
215000
-
gel filtration
Clostridium kluyveri
220000
-
equilibrium sedimentation
Clostridium kluyveri
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-acetoacetyl-CoA + NADPH + H+
Clostridium kluyveri
synthesis of butyrate
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium kluyveri
-
-
-
Purification (Commentary)
Commentary
Organism
-
Clostridium kluyveri
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
445
-
reduction of 3-acetoacetyl-CoA, pH 6.5, 25°C
Clostridium kluyveri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-acetoacetyl-CoA + NADPH + H+
synthesis of butyrate
286053
Clostridium kluyveri
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
-
?
3-acetoacetyl-CoA + NADPH + H+
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
286053
Clostridium kluyveri
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
-
r
Subunits
Subunits
Commentary
Organism
octamer
8 * 26000, SDS-PAGE
Clostridium kluyveri
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Clostridium kluyveri
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
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
Clostridium kluyveri
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
Clostridium kluyveri
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
7.5
pH 5: about 35% of maximal activity, pH 7.5: about 55% of maximal activity, reduction of 3-acetoacetyl-CoA
Clostridium kluyveri
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Clostridium kluyveri
NADPH
the rate with NADH is below 0.25% of that with NADPH
Clostridium kluyveri
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Clostridium kluyveri
NADPH
the rate with NADH is below 0.25% of that with NADPH
Clostridium kluyveri
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoic acid)
0.05 mM, 80% inhibition
Clostridium kluyveri
iodoacetamide
1 mM, slight inhibition
Clostridium kluyveri
N-ethylmaleimide
1 mM, slight inhibition
Clostridium kluyveri
p-chloromercuribenzoate
1 mM, complete inhibition
Clostridium kluyveri
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.05
-
3-acetoacetyl-CoA
pH 6.5, 25°C
Clostridium kluyveri
0.07
-
NADPH
pH 6.5, 25°C
Clostridium kluyveri
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
8 * 26000, SDS-PAGE
Clostridium kluyveri
215000
-
gel filtration
Clostridium kluyveri
220000
-
equilibrium sedimentation
Clostridium kluyveri
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-acetoacetyl-CoA + NADPH + H+
Clostridium kluyveri
synthesis of butyrate
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Clostridium kluyveri
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
445
-
reduction of 3-acetoacetyl-CoA, pH 6.5, 25°C
Clostridium kluyveri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-acetoacetyl-CoA + NADPH + H+
synthesis of butyrate
286053
Clostridium kluyveri
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
-
?
3-acetoacetyl-CoA + NADPH + H+
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
286053
Clostridium kluyveri
(S)-3-hydroxybutanoyl-CoA + NADP+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
octamer
8 * 26000, SDS-PAGE
Clostridium kluyveri
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Clostridium kluyveri
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
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
Clostridium kluyveri
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
Clostridium kluyveri
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
7.5
pH 5: about 35% of maximal activity, pH 7.5: about 55% of maximal activity, reduction of 3-acetoacetyl-CoA
Clostridium kluyveri
Other publictions for EC 1.1.1.157
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
726748
Hawkins
Conversion of 4-hydroxybutyrat ...
Metallosphaera sedula, Metallosphaera sedula DSM 5348
Appl. Environ. Microbiol.
80
2536-2545
2014
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3
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286046
Hartmanis
Selenomethionine-containing th ...
Clostridium kluyveri
Curr. Top. Cell. Regul.
27
479-486
1985
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1
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2
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1
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1
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1
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1
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1
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1
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1
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1
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1
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1
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1
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-
286047
Sliwkowski
Simultaneous single-step purif ...
Clostridium kluyveri
Anal. Biochem.
141
344-347
1984
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1
1
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2
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1
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1
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2
1
1
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1
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1
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1
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1
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1
1
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1
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1
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2
1
1
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-
1
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1
-
-
-
-
-
-
286053
Madan
Purification and properties of ...
Clostridium kluyveri
Eur. J. Biochem.
32
51-56
1973
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4
2
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-
3
1
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2
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1
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1
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2
1
1
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2
1
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2
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2
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4
-
2
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3
1
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1
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1
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2
1
1
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2
1
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