BRENDA - Enzyme Database
show all sequences of 1.2.1.25

Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched chain alpha-keto acid dehydrogenase. I. Purification and properties of the enzyme from Bacillus subtilis

Namba, Y.; Yoshizawa, K.; Ejima, A.; Hayashi, T.; Kaneda, T.; J. Biol. Chem. 244, 4437-4447 (1969)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
2-oxoisopentanoate
competitive
Bacillus subtilis
iodoacetate
-
Bacillus subtilis
L-2-Oxo-3-methylpentanoate
competitive
Bacillus subtilis
NEM
-
Bacillus subtilis
PCMB
-
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
CoA
-
Bacillus subtilis
1.66
-
L-alpha-keto-beta-methylvalerate
-
Bacillus subtilis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Purification (Commentary)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-methyl-2-oxobutanoate + CoA + NAD+
specific for the L-isomer
390216
Bacillus subtilis
2-methylpropanoyl-CoA + CO2 + NADH
-
390216
Bacillus subtilis
?
4-methyl-2-oxopentanoate + CoA + NAD+
-
390216
Bacillus subtilis
3-methyl-butanoyl-CoA + CO2 + NADH
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Bacillus subtilis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
7.5
pH 6.0: about 25% of maximal activity, pH 7.5: about 45% of maximal activity
Bacillus subtilis
Cofactor
Cofactor
Commentary
Organism
Structure
CoA
required
Bacillus subtilis
additional information
CoA and NAD+ can be replaced by potassium ferricyanide but the activity is much lower; enzyme probably identical with EC 1.2.4.4
Bacillus subtilis
NAD+
required
Bacillus subtilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
CoA
required
Bacillus subtilis
additional information
CoA and NAD+ can be replaced by potassium ferricyanide but the activity is much lower; enzyme probably identical with EC 1.2.4.4
Bacillus subtilis
NAD+
required
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-oxoisopentanoate
competitive
Bacillus subtilis
iodoacetate
-
Bacillus subtilis
L-2-Oxo-3-methylpentanoate
competitive
Bacillus subtilis
NEM
-
Bacillus subtilis
PCMB
-
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
CoA
-
Bacillus subtilis
1.66
-
L-alpha-keto-beta-methylvalerate
-
Bacillus subtilis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-methyl-2-oxobutanoate + CoA + NAD+
specific for the L-isomer
390216
Bacillus subtilis
2-methylpropanoyl-CoA + CO2 + NADH
-
390216
Bacillus subtilis
?
4-methyl-2-oxopentanoate + CoA + NAD+
-
390216
Bacillus subtilis
3-methyl-butanoyl-CoA + CO2 + NADH
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Bacillus subtilis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
7.5
pH 6.0: about 25% of maximal activity, pH 7.5: about 45% of maximal activity
Bacillus subtilis
Other publictions for EC 1.2.1.25
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)
735476
Ganesan
Identification of the leucine- ...
Lactococcus lactis, Lactococcus lactis IL1403
Appl. Environ. Microbiol.
72
4264-4273
2006
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10
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1
1
1
1
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-
390216
Namba
Coenzyme A- and nicotinamide a ...
Bacillus subtilis
J. Biol. Chem.
244
4437-4447
1969
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5
2
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-
1
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1
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2
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1
1
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3
-
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3
-
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5
-
2
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
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-
1
1
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