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(indol-3-yl)pyruvate
(indol-3-yl)acetaldehyde + CO2
2-oxo-3-methylpentanoate
2-methylbutanal + CO2
-
-
-
?
2-oxo-3-methylvalerate
2-methylbutanal + CO2
-
the enzymatic activity toward 2-oxo-3-methylvalerate is 1.5times higher than the activity toward 2-oxo-isovalerate
-
-
?
2-oxo-3-phenylpropanoic acid
phenylacetaldehyde + CO2
-
at 30 mM 8.6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
2-oxobutanoate
propanal + CO2
-
-
-
?
2-oxobutanoic acid
propanal + CO2
2-oxobutyrate
propionaldehyde + CO2
-
-
-
?
2-oxoglutarate
CO2 + succinate semialdehyde
-
5% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
2-oxohexanoate
n-pentanal + CO2
-
-
-
?
2-oxohexanoic acid
pentanal + CO2
2-oxoisocaproate
3-methylbutanal + CO2
2-oxoisohexanoate
? + CO2
-
-
-
?
2-oxoisohexanoate
CO2 + isopentanal
2-oxoisopentanoate
2-methylpropanal + CO2
-
-
-
?
2-oxoisopentanoate
CO2 + isobutanal
-
63% of the activity with L-3-methyl-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
2-oxoisovalerate
isobutanal + CO2
2-oxomethylvalerate
pentanal + CO2
2-oxopentanoate
butanal + CO2
-
-
-
?
2-oxopentanoate
n-butanal + CO2
-
-
-
?
2-oxopentanoic acid
butanal + CO2
2-oxopropanoic acid
acetaldehyde + CO2
-
at 30 mM 1.2% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
3,5-dimethoxybenzaldehyde + 2-oxopropanoic acid
(1R)-1-(3,5-dimethoxyphenyl)-1-hydroxypropan-2-one + CO2
-
-
-
-
?
3-(4-hydroxyphenyl)-2-oxopropanoic acid
(4-hydroxyphenyl)-acetaldehyde + CO2
-
at 30 mM 6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
3-formylbenzonitrile + 2-oxobutanoic acid
3-[(1R)-1-hydroxy-2-oxobutyl]benzonitrile
-
-
-
-
?
3-methyl-2-oxobutanoate
2-methylpropanal + CO2
3-methyl-2-oxobutanoic acid
2-methylpropanal + CO2
3-methyl-2-oxobutyrate
3-methylpropanal + CO2
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
4-(4-hydroxyphenyl)-2-oxobutanoic acid
3-(4-hydroxyphenyl)-propanal + CO2
-
at 30 mM 1.6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-(methylsulfanyl)-2-oxobutanoic acid
3-(methylsulfanyl)-propanal + CO2
-
at 30 mM 18% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
4-methyl-2-oxohexanoic acid
3-methylpentanal + CO2
-
at 30 mM 19% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
4-methylthio-2-oxobutanoate
3-methylthiopropanal + CO2
4-methylthio-2-oxobutanoic acid
3-methylthiopropanal + CO2
10% of the rate with 3-methyl-2-oxobutanoic acid
-
-
?
5-(4-hydroxyphenyl)-2-oxopentanoic acid
4-(4-hydroxyphenyl)-butanal + CO2
-
at 30 mM 1.1% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
alpha-isocaproic acid
3-methylbutanal + CO2
-
-
-
?
benzaldehyde + CO2
(R)-benzoin
-
self-carboligation
-
-
?
benzoylformate
? + CO2
-
-
-
?
indole-3-pyruvate
?
-
at 1 mM 0.85% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
isovaleraldehyde
?
-
self-carboligation
-
-
?
L-3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
oxo(phenyl)acetic acid
benzaldehyde + CO2
-
at 30 mM 8.4% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
pyruvate
acetaldehyde + CO2
additional information
?
-
(indol-3-yl)pyruvate
(indol-3-yl)acetaldehyde + CO2
-
-
-
?
(indol-3-yl)pyruvate
(indol-3-yl)acetaldehyde + CO2
-
-
-
?
2-oxobutanoic acid
propanal + CO2
10% of the rate with 3-methyl-2-oxobutanoic acid
-
-
?
2-oxobutanoic acid
propanal + CO2
-
at 30 mM 9.3% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
2-oxohexanoic acid
pentanal + CO2
30% of the rate with 3-methyl-2-oxobutanoic acid
-
-
?
2-oxohexanoic acid
pentanal + CO2
-
at 30 mM 13% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
-
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
-
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
22.7% of the activity with 2-oxoisovalerate
-
-
?
2-oxoisohexanoate
CO2 + isopentanal
-
38% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
2-oxoisohexanoate
CO2 + isopentanal
-
38% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
?
2-oxoisovalerate
isobutanal + CO2
-
-
-
?
2-oxoisovalerate
isobutanal + CO2
-
-
-
?
2-oxomethylvalerate
pentanal + CO2
-
-
-
?
2-oxomethylvalerate
pentanal + CO2
16.7% of the activity with 2-oxoisovalerate
-
-
?
2-oxopentanoic acid
butanal + CO2
25% of the rate with 3-methyl-2-oxobutanoic acid
-
-
?
2-oxopentanoic acid
butanal + CO2
-
at 30 mM 15% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
3-methyl-2-oxobutanoate
2-methylpropanal + CO2
-
-
-
?
3-methyl-2-oxobutanoate
2-methylpropanal + CO2
-
-
-
?
3-methyl-2-oxobutanoic acid
2-methylpropanal + CO2
-
-
-
-
?
3-methyl-2-oxobutanoic acid
2-methylpropanal + CO2
-
-
-
?
3-methyl-2-oxobutanoic acid
2-methylpropanal + CO2
-
100% activity
-
-
?
3-methyl-2-oxobutyrate
3-methylpropanal + CO2
-
-
-
-
?
3-methyl-2-oxobutyrate
3-methylpropanal + CO2
-
-
-
-
?
3-methyl-2-oxobutyrate
3-methylpropanal + CO2
-
-
-
-
?
3-methyl-2-oxobutyrate
3-methylpropanal + CO2
-
-
-
-
?
3-methyl-2-oxobutyrate
3-methylpropanal + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
-
-
-
?
3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
-
-
-
-
?
3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
-
-
-
-
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
30% of the rate with 3-methyl-2-oxobutanoic acid
-
-
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
-
at 30 mM 38.1% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
-
-
-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
-
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
-
-
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
-
-
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
-
-
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
-
-
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
-
-
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
-
-
-
?
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
35% of the rate with 3-methyl-2-oxobutanoic acid
-
-
?
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
-
at 30 mM 26.3% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-methylthio-2-oxobutanoate
3-methylthiopropanal + CO2
-
-
-
?
4-methylthio-2-oxobutanoate
3-methylthiopropanal + CO2
-
-
-
?
L-3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
-
stereospecificity towards the L-isomer
-
-
?
L-3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
8.8% of the activity with 2-oxoisovalerate
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
ethanal + CO2
-
25% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
pyruvate
ethanal + CO2
-
-
-
-
?
pyruvate
ethanal + CO2
-
-
-
-
?
pyruvate
ethanal + CO2
-
-
-
-
?
pyruvate
ethanal + CO2
-
-
-
-
?
pyruvate
ethanal + CO2
-
-
-
-
?
additional information
?
-
-
essential for the synthesis of branched-chain fatty acids
-
-
?
additional information
?
-
-
plants with enzymic activity show enhanced cold tolerance, role as a protective mechanism for growth of plants under sub optimal temperatures
-
-
?
additional information
?
-
acetolactate synthase AlsS, EC 2.2.1.6, is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro
-
-
?
additional information
?
-
acetolactate synthase AlsS, EC 2.2.1.6, is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro
-
-
?
additional information
?
-
-
3-fluoro-2-oxopropanoic acid, isobutyraldehyde, 3,5-dichlorobenzaldehyde, 3,5-dimethoxybenzaldehyde and 2-oxooctanoic acid are no substrates
-
-
?
additional information
?
-
-
the enzyme is also able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C-C bond formation, in particular for the enzymatic synthesis of diversely substituted 2-hydroxyketones with high enantioselectivity
-
-
?
additional information
?
-
-
enzyme additionallly catalyzes the asymmetric synthesis of chiral 2-hydroxy ketones with high stereochemical purity
-
-
?
additional information
?
-
very poor substrates: indole-3-pyruvate and pyruvate
-
-
?
additional information
?
-
enzyme is found to convert a broad spectrum of branched-chain and aromatic alpha-keto acids. Determined the catalytic constants for the conversion of 11 aliphatic, aromatic, and branched-chain alpha-keto acids
-
-
?
additional information
?
-
-
enzyme is found to convert a broad spectrum of branched-chain and aromatic alpha-keto acids. Determined the catalytic constants for the conversion of 11 aliphatic, aromatic, and branched-chain alpha-keto acids
-
-
?
additional information
?
-
enzyme is found to convert a broad spectrum of branched-chain and aromatic alpha-keto acids. Determined the catalytic constants for the conversion of 11 aliphatic, aromatic, and branched-chain alpha-keto acids
-
-
?
additional information
?
-
-
enzyme is found to convert a broad spectrum of branched-chain and aromatic alpha-keto acids. Determined the catalytic constants for the conversion of 11 aliphatic, aromatic, and branched-chain alpha-keto acids
-
-
?
additional information
?
-
-
mitochondrial branched-chain aminotransferase binds to the E1 decarboxylase of BCKDC, forming a metabolon that allows channeling of branched-chain alpha-keto acids from mitochondrial branched-chain aminotransferase to E1
-
-
?
additional information
?
-
no activity with 2-oxoglutarate
-
-
?
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Acidosis
Acidosis and glucocorticoids induce branched-chain amino acid catabolism.
Acidosis
Chronic metabolic acidosis accelerates whole body proteolysis and oxidation in awake rats.
Acidosis
Glucocorticoids and acidification independently increase transcription of branched-chain ketoacid dehydrogenase subunit genes.
Acidosis
Mechanisms contributing to muscle-wasting in acute uremia: activation of amino acid catabolism.
Acidosis
Mechanisms for protein catabolism in uremia: metabolic acidosis and activation of proteolytic pathways.
Acidosis
Metabolic acidosis accelerates whole body protein degradation and leucine oxidation by a glucocorticoid-dependent mechanism.
Acidosis
Tissue-specific responses of branched-chain alpha-ketoacid dehydrogenase activity in metabolic acidosis.
Brain Diseases
Living donor liver transplantation in maple syrup urine disease - Case series and world's youngest domino liver donor and recipient.
branched-chain-2-oxoacid decarboxylase deficiency
Demonstration of a new mammalian isoleucine catabolic pathway yielding an Rseries of metabolites.
Carcinoma, Hepatocellular
Regulation of expression of branched-chain alpha-keto acid dehydrogenase subunits in permanent cell lines.
Maple Syrup Urine Disease
A distinct variant of intermediate maple syrup urine disease.
Maple Syrup Urine Disease
Altered kinetic properties of the branched-chain alpha-keto acid dehydrogenase complex due to mutation of the beta-subunit of the branched-chain alpha-keto acid decarboxylase (E1) component in lymphoblastoid cells derived from patients with maple syrup urine disease.
Maple Syrup Urine Disease
Maple syrup urine disease: branched-chain keto acid decarboxylation in fibroblasts as measured with amino acids and keto acids.
Neoplasms
Administration of endotoxin, tumor necrosis factor, or interleukin 1 to rats activates skeletal muscle branched-chain alpha-keto acid dehydrogenase.
Sepsis
Administration of endotoxin, tumor necrosis factor, or interleukin 1 to rats activates skeletal muscle branched-chain alpha-keto acid dehydrogenase.
Starvation
Effect of starvation on branched-chain alpha-keto acid dehydrogenase activity in rat heart and skeletal muscle.
Tuberculosis
Amino acids allosterically regulate the thiamine diphosphate-dependent alpha-keto acid decarboxylase from Mycobacterium tuberculosis.
Uremia
Glucocorticoids and acidification independently increase transcription of branched-chain ketoacid dehydrogenase subunit genes.
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0.09
(indol-3-yl)pyruvate
-
20.25
2-oxo-3-methylpentanoate
-
0.127
2-oxo-3-phenylpropanoate
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
5.58
2-oxobutanoate
Hill coefficient 1.1, pH 7.0, 30°C
0.6
2-oxohexanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.57
2-oxoisocaproate
Hill coefficient 1.0, pH 7.0, 30°C
2
2-Oxoisohexanoate
-
25°C, pH 7.2
0.05 - 342
2-oxoisovalerate
3.49
2-oxomethylvalerate
Hill coefficient 0.8, pH 7.0, 30°C
1.21 - 1.44
2-oxopentanoate
1.3
2-oxopentanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
29.77
2-Oxopropanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.63
3-(4-hydroxyphenyl)-2-oxopropanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.027 - 14.6
3-methyl-2-oxobutanoate
5.02
3-methyl-2-oxobutanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.1 - 0.87
3-methyl-2-oxopentanoate
1.3
4-(methylsulfanyl)-2-oxobutanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.042
4-methyl-2-oxopentanoate
pH 7.0, 55°C
0.264
4-methyl-2-oxopentanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
1.43
4-methylthio-2-oxobutanoate
Hill coefficient 1.1, pH 7.0, 30°C
0.234
Indole-3-pyruvate
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.001
L-3-Methyl-2-oxopentanoate
-
and 2-oxoisopentanoate, 2-oxoisohexanoate, value below, 30°C, pH 7.5
7.5
oxo(phenyl)acetic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.2 - 1.17
phenylpyruvate
0.00063 - 0.04
thiamine diphosphate
0.05
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.05
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, overall reaction
0.05
2-oxoisovalerate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.05
2-oxoisovalerate
-
wild-type, pH 7.5, 30°C, overall reaction
0.14
2-oxoisovalerate
-
mutant Y300A, pH 7.5, 30°C, overall reaction
0.225
2-oxoisovalerate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.252
2-oxoisovalerate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.255
2-oxoisovalerate
-
mutant R301A, pH 7.5, 30°C, overall reaction
0.337
2-oxoisovalerate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.39
2-oxoisovalerate
-
mutant Y300F, pH 7.5, 30°C, overall reaction
1.9
2-oxoisovalerate
pH 6.5, 37°C
8.31
2-oxoisovalerate
Hill coefficient 0.9, pH 7.0, 30°C
154
2-oxoisovalerate
mutant Q487S, pH 7.0, 37°C
175
2-oxoisovalerate
mutant Q487G, pH 7.0, 37°C
186
2-oxoisovalerate
mutant Q487A, pH 7.0, 37°C
300
2-oxoisovalerate
wild-type, pH 7.0, 37°C
323
2-oxoisovalerate
mutant Q487I, pH 7.0, 37°C
342
2-oxoisovalerate
mutant Q487L, pH 7.0, 37°C
1.21
2-oxopentanoate
-
1.44
2-oxopentanoate
Hill coefficient 1.1, pH 7.0, 30°C
0.027
3-methyl-2-oxobutanoate
pH 7.0, 55°C
2.6
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/I404C, pH 6.5, 30°C
5.1
3-methyl-2-oxobutanoate
wild-type, pH 6.5, 30°C
5.2
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290C, pH 6.5, 30°C
5.6
3-methyl-2-oxobutanoate
mutant V461I, pH 6.5, 30°C
6.6
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290V, pH 6.5, 30°C
8.6
3-methyl-2-oxobutanoate
mutant A290M/Q252N/D306G/E316R/F388Y/L434C, pH 6.5, 30°C
9.3
3-methyl-2-oxobutanoate
mutant V461I/A290M, pH 6.5, 30°C
14.6
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y, pH 6.5, 30°C
0.1
3-methyl-2-oxopentanoate
pH 7.0, 55°C
0.87
3-methyl-2-oxopentanoate
-
25°C, pH 7.2
0.2
phenylpyruvate
Hill coefficient 1.0, pH 7.0, 30°C
0.4
pyruvate
-
0.6
pyruvate
pH 7.0, 55°C
33
pyruvate
Hill coefficient 1.2, pH 7.0, 30°C
0.00063
thiamine diphosphate
-
wild-type, pH 7.5, 30°C, overall reaction
0.0066
thiamine diphosphate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.015
thiamine diphosphate
-
mutant D295A, pH 7.5, 30°C, overall reaction
0.016
thiamine diphosphate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.018
thiamine diphosphate
-
mutant Y300F, pH 7.5, 30°C, overall reaction
0.026
thiamine diphosphate
-
mutant R301A, pH 7.5, 30°C, overall reaction
0.026
thiamine diphosphate
-
mutant Y300A, pH 7.5, 30°C, overall reaction
0.028
thiamine diphosphate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.029
thiamine diphosphate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.04
thiamine diphosphate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.98
(indol-3-yl)pyruvate
-
19.75
2-oxo-3-methylpentanoate
-
28.35
2-oxoisopentanoate
-
0.19 - 8.9
2-oxoisovalerate
0.3 - 149
3-methyl-2-oxobutanoate
29 - 33
3-methyl-2-oxobutyrate
0.5 - 27
3-methyl-2-oxopentanoate
3.89
4-hydroxyphenylpyruvate
-
0.17 - 8.5
4-methyl-2-oxopentanoate
0.19 - 0.53
thiamine diphosphate
0.19
2-oxoisovalerate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.19
2-oxoisovalerate
-
wild-type, pH 7.5, 30°C, overall reaction
0.38
2-oxoisovalerate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.38
2-oxoisovalerate
-
mutant Y300A, pH 7.5, 30°C, overall reaction
0.41
2-oxoisovalerate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.41
2-oxoisovalerate
-
mutant R301A, pH 7.5, 30°C, overall reaction
0.48
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.48
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, overall reaction
0.57
2-oxoisovalerate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.57
2-oxoisovalerate
-
mutant Y300F, pH 7.5, 30°C, overall reaction
0.8
2-oxoisovalerate
mutant Q487G, pH 7.0, 37°C
0.8
2-oxoisovalerate
mutant Q487S, pH 7.0, 37°C
1.1
2-oxoisovalerate
mutant Q487A, pH 7.0, 37°C
4.8
2-oxoisovalerate
mutant Q487I, pH 7.0, 37°C
5.4
2-oxoisovalerate
mutant Q487L, pH 7.0, 37°C
8.9
2-oxoisovalerate
wild-type, pH 7.0, 37°C
0.3
3-methyl-2-oxobutanoate
pH 7.0, 55°C
5.2
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/I404C, pH 6.5, 30°C
43
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290V, pH 6.5, 30°C
69
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290C, pH 6.5, 30°C
95
3-methyl-2-oxobutanoate
mutant A290M/Q252N/D306G/E316R/F388Y/L434C, pH 6.5, 30°C
118
3-methyl-2-oxobutanoate
mutant V461I/A290M, pH 6.5, 30°C
120
3-methyl-2-oxobutanoate
mutant V461I, pH 6.5, 30°C
145
3-methyl-2-oxobutanoate
wild-type, pH 6.5, 30°C
149
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y, pH 6.5, 30°C
29
3-methyl-2-oxobutyrate
-
pH and temperature not specified in the publication
33
3-methyl-2-oxobutyrate
-
pH and temperature not specified in the publication
0.5
3-methyl-2-oxopentanoate
pH 7.0, 55°C
23
3-methyl-2-oxopentanoate
-
pH and temperature not specified in the publication
25
3-methyl-2-oxopentanoate
-
pH and temperature not specified in the publication
27
3-methyl-2-oxopentanoate
-
pH and temperature not specified in the publication
0.17
4-methyl-2-oxopentanoate
pH 7.0, 55°C
7
4-methyl-2-oxopentanoate
-
pH and temperature not specified in the publication
8.5
4-methyl-2-oxopentanoate
-
pH and temperature not specified in the publication
1.7
phenylpyruvate
-
pH and temperature not specified in the publication
1.8
phenylpyruvate
-
pH and temperature not specified in the publication
0.09
pyruvate
pH 7.0, 55°C
0.19
thiamine diphosphate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.19
thiamine diphosphate
-
wild-type, pH 7.5, 30°C, overall reaction
0.31
thiamine diphosphate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.31
thiamine diphosphate
-
mutant Y300A, pH 7.5, 30°C, overall reaction
0.41
thiamine diphosphate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.41
thiamine diphosphate
-
mutant R301A, pH 7.5, 30°C, overall reaction
0.42
thiamine diphosphate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.42
thiamine diphosphate
-
mutant D295A, pH 7.5, 30°C, overall reaction
0.53
thiamine diphosphate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.53
thiamine diphosphate
-
mutant Y300F, pH 7.5, 30°C, overall reaction
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THI3_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
609
0
68366
Swiss-Prot
other Location (Reliability: 5)
PDC5_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
563
0
61912
Swiss-Prot
other Location (Reliability: 1)
PDC6_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
563
0
61580
Swiss-Prot
other Location (Reliability: 2)
PDC1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
563
0
61495
Swiss-Prot
other Location (Reliability: 1)
ARO10_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
635
1
71384
Swiss-Prot
other Location (Reliability: 2)
A0A6C1E4B3_SACPS
620
0
69771
TrEMBL
other Location (Reliability: 3)
A0A6C1DVV6_SACPS
563
0
61495
TrEMBL
other Location (Reliability: 1)
A0A8B8URL6_SACPA
563
0
61509
TrEMBL
other Location (Reliability: 2)
G2WEH1_YEASK
Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557)
436
0
47872
TrEMBL
other Location (Reliability: 1)
C8ZD16_YEAS8
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
563
0
61529
TrEMBL
other Location (Reliability: 1)
N1P0G2_YEASC
Saccharomyces cerevisiae (strain CEN.PK113-7D)
563
0
61510
TrEMBL
other Location (Reliability: 1)
J8Q5B5_SACAR
Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644)
563
0
61594
TrEMBL
other Location (Reliability: 1)
B3LT95_YEAS1
Saccharomyces cerevisiae (strain RM11-1a)
563
0
61942
TrEMBL
other Location (Reliability: 1)
A0A6C1DPC1_SACPS
580
0
64977
TrEMBL
other Location (Reliability: 2)
B5VJ31_YEAS6
Saccharomyces cerevisiae (strain AWRI1631)
493
0
53848
TrEMBL
other Location (Reliability: 2)
A0A0L8VTN5_9SACH
635
1
71384
TrEMBL
other Location (Reliability: 2)
A0A6C1DPY0_SACPS
635
1
71271
TrEMBL
other Location (Reliability: 2)
C7GU46_YEAS2
Saccharomyces cerevisiae (strain JAY291)
426
0
46768
TrEMBL
other Location (Reliability: 2)
A0A0L8RP53_SACEU
635
1
71543
TrEMBL
other Location (Reliability: 2)
M4X0E1_YEASX
635
1
71384
TrEMBL
other Location (Reliability: 2)
C8Z5U4_YEAS8
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
635
1
71418
TrEMBL
other Location (Reliability: 2)
C8Z8Y1_YEAS8
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
563
0
61564
TrEMBL
other Location (Reliability: 2)
J6EG81_SACK1
Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889)
620
0
69690
TrEMBL
other Location (Reliability: 3)
J6EER6_SACK1
Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889)
635
0
71342
TrEMBL
other Location (Reliability: 2)
A0A0L8REF5_SACEU
563
0
61492
TrEMBL
other Location (Reliability: 1)
B3LT15_YEAS1
Saccharomyces cerevisiae (strain RM11-1a)
563
0
61495
TrEMBL
other Location (Reliability: 1)
A0A0L8VQ53_9SACH
563
0
61580
TrEMBL
other Location (Reliability: 2)
A0A6C1EBJ7_SACPS
563
0
61492
TrEMBL
other Location (Reliability: 1)
A7A0U9_YEAS7
Saccharomyces cerevisiae (strain YJM789)
563
0
61495
TrEMBL
other Location (Reliability: 1)
A0A6C1E317_SACPS
635
1
71509
TrEMBL
other Location (Reliability: 2)
A0A8H8UMK7_YEASX
609
0
68366
TrEMBL
other Location (Reliability: 5)
A0A166MTJ5_YEASX
635
1
71412
TrEMBL
other Location (Reliability: 2)
G2WIN6_YEASK
Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557)
563
0
61509
TrEMBL
other Location (Reliability: 1)
C8Z4J0_YEAS8
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
621
0
69755
TrEMBL
other Location (Reliability: 5)
H0GGK8_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
563
0
61564
TrEMBL
other Location (Reliability: 2)
A0A8B8UW02_SACPA
563
0
61845
TrEMBL
other Location (Reliability: 1)
A0A0L8VKT7_9SACH
563
0
61912
TrEMBL
other Location (Reliability: 1)
B5VGQ7_YEAS6
Saccharomyces cerevisiae (strain AWRI1631)
621
0
69812
TrEMBL
other Location (Reliability: 2)
J5RSE2_SACK1
Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889)
563
0
61967
TrEMBL
other Location (Reliability: 2)
A0A0L8VLD5_9SACH
563
0
61495
TrEMBL
other Location (Reliability: 1)
H0GK16_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
563
0
61495
TrEMBL
other Location (Reliability: 1)
H0GDR7_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
621
0
69752
TrEMBL
other Location (Reliability: 5)
B5VN63_YEAS6
Saccharomyces cerevisiae (strain AWRI1631)
258
0
28916
TrEMBL
other Location (Reliability: 2)
A0A6C1DWX6_SACPS
563
0
61903
TrEMBL
other Location (Reliability: 1)
A0A8H4F8E8_YEASX
563
0
61912
TrEMBL
other Location (Reliability: 1)
A0A5Q2WV56_YEASX
563
0
61494
TrEMBL
other Location (Reliability: 1)
N1P9V9_YEASC
Saccharomyces cerevisiae (strain CEN.PK113-7D)
563
0
61533
TrEMBL
other Location (Reliability: 2)
A0A2X0Q412_9LACT
457
0
50517
TrEMBL
-
C8ZDA3_YEAS8
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
563
0
61912
TrEMBL
other Location (Reliability: 1)
M4WIW8_YEASX
635
1
71418
TrEMBL
other Location (Reliability: 2)
C7GJN2_YEAS2
Saccharomyces cerevisiae (strain JAY291)
580
0
64935
TrEMBL
other Location (Reliability: 2)
A0A8B8UVM8_SACPA
563
0
61483
TrEMBL
other Location (Reliability: 1)
J8PY16_SACAR
Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644)
635
1
71349
TrEMBL
other Location (Reliability: 2)
B3LID9_YEAS1
Saccharomyces cerevisiae (strain RM11-1a)
563
0
61564
TrEMBL
other Location (Reliability: 2)
H0GXZ9_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
563
0
61384
TrEMBL
other Location (Reliability: 1)
A7A133_YEAS7
Saccharomyces cerevisiae (strain YJM789)
563
0
61903
TrEMBL
other Location (Reliability: 1)
A0A0L8RJ93_SACEU
563
0
61745
TrEMBL
other Location (Reliability: 2)
A0A8B8UN47_SACPA
621
0
69823
TrEMBL
other Location (Reliability: 5)
J8Q4X5_SACAR
Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644)
563
0
61870
TrEMBL
other Location (Reliability: 2)
G2WC83_YEASK
Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557)
621
0
69740
TrEMBL
other Location (Reliability: 2)
H0GY93_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
563
0
61967
TrEMBL
other Location (Reliability: 2)
A0A7I9FNH9_YEASX
563
0
61495
TrEMBL
other Location (Reliability: 1)
A6ZXP8_YEAS7
Saccharomyces cerevisiae (strain YJM789)
621
0
69755
TrEMBL
other Location (Reliability: 5)
G2WIX3_YEASK
Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557)
563
0
61903
TrEMBL
other Location (Reliability: 1)
N1P457_YEASC
Saccharomyces cerevisiae (strain CEN.PK113-7D)
609
0
68366
TrEMBL
other Location (Reliability: 5)
A0A6C1DSN7_SACPS
563
0
61608
TrEMBL
other Location (Reliability: 2)
J8PZD7_SACAR
Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644)
563
0
61875
TrEMBL
other Location (Reliability: 2)
B5VFI6_YEAS6
Saccharomyces cerevisiae (strain AWRI1631)
446
0
50404
TrEMBL
other Location (Reliability: 2)
A6ZV69_YEAS7
Saccharomyces cerevisiae (strain YJM789)
563
0
61580
TrEMBL
other Location (Reliability: 2)
A6ZYY0_YEAS7
Saccharomyces cerevisiae (strain YJM789)
635
1
71384
TrEMBL
other Location (Reliability: 2)
A0A8B8UPB8_SACPA
635
1
71636
TrEMBL
other Location (Reliability: 2)
A0A0L8VSJ3_9SACH
621
0
69755
TrEMBL
other Location (Reliability: 5)
H0GEJ2_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
635
1
71384
TrEMBL
other Location (Reliability: 2)
N1P7B5_YEASC
Saccharomyces cerevisiae (strain CEN.PK113-7D)
635
1
71384
TrEMBL
other Location (Reliability: 2)
H0GK91_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
563
0
61912
TrEMBL
other Location (Reliability: 1)
A0A6C1E8A3_SACPS
563
0
61730
TrEMBL
other Location (Reliability: 2)
A0A6C1EC67_SACPS
563
0
61778
TrEMBL
other Location (Reliability: 2)
A0A8H4C1R4_YEASX
563
0
61580
TrEMBL
other Location (Reliability: 2)
C7GWX6_YEAS2
Saccharomyces cerevisiae (strain JAY291)
563
0
61580
TrEMBL
other Location (Reliability: 2)
C7GMF5_YEAS2
Saccharomyces cerevisiae (strain JAY291)
635
1
71357
TrEMBL
other Location (Reliability: 2)
G2WBB9_YEASK
Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557)
259
1
29112
TrEMBL
other Location (Reliability: 2)
A0A0L8RF52_SACEU
563
0
61778
TrEMBL
other Location (Reliability: 2)
A0A0L8RLH3_SACEU
620
0
69771
TrEMBL
other Location (Reliability: 3)
B3LFS1_YEAS1
Saccharomyces cerevisiae (strain RM11-1a)
635
1
71314
TrEMBL
other Location (Reliability: 2)
KDC_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
560
0
59783
Swiss-Prot
-
ILVX_BACSU
Bacillus subtilis (strain 168)
570
0
62004
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q684J7_LACLL
548
0
60948
TrEMBL
-
Q6QBS4_9LACT
547
0
60884
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Q487A
mutation diminishes the decarboxylase activity but maintains the acetolactate synthase activity
Q487G
mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487I
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487L
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487S
mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
A240P-alpha
-
slow assembly of alpha2beta2 tetramer
D295A
-
of component E1b, 2fold increase in kcat-value
E193A-alpha
-
complete inactivation of enzyme
E76A-beta
-
complete inactivation of enzyme
F364C-alpha
-
slow assembly of enzyme, alphabeta dimer
G204S-alpha
-
slow assembly of alpha2beta2 tetramer
G245R-alpha
-
moderately slow assembly of alpha2beta2 tetramer
H146A-beta
-
complete inactivation of enzyme
H291A-alpha
-
partially active enzyme
R114W-alpha
-
naturally occuring mutation in maple syrup disease patients, strongly reduced binding of thiamin diphosphate, enzyme inactive
R287A
-
of component E1b, 40fold increase in Km-value for 2-oxoisovalerate
R301A
-
of component E1b, 4fold increase in Km-value for 2-oxoisovalerate
T166M-alpha
-
enzyme inactive, with attenuated ability to bind thiamin diphosphate
T265R
-
no assembly of alpha2beta2 tetramer
Y224A-alpha
-
markedly higher Km value for thiamin diphosphate
Y300A
-
of component E1b, 6fold increase in Km-value for 2-oxoisovalerate
Y300F
-
of component E1b, 5fold increase in Km-value for 2-oxoisovalerate
Y368C-alpha
-
slow assembly of enzyme as alphabeta dimer and alpha2beta2 tetramer
V461I
3.3 degrees increase in thermostability compared to wild-type
V461I/A290M
increase in thermostability compared to wild-type
V461I/A290M/Q252N/D306G/E316R/F388Y
increase in thermostability compared to wild-type
V461I/A290M/Q252N/D306G/E316R/F388Y/I404C
increase in thermostability compared to wild-type
V461I/A290M/Q252N/D306G/E316R/F388Y/L434C
increase in thermostability compared to wild-type
V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290C
greater than 400fold improvement of half-life at 70°C and greater than 600fold increase in process stability in the presence of 4% isobutanol at 50°C
V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290V
increase in thermostability compared to wild-type
N222S-alpha
-
markedly higher Km value for thiamin diphosphate
N222S-alpha
-
normal assembly of alpha2beta2 tetramer
R220W-alpha
-
normal assembly of alpha2beta2 tetramer
R220W-alpha
-
naturally occuring mutation in maple syrup disease patients, strongly reduced binding of thiamin diphosphate, enzyme inactive
Y393N-alpha
-
slow assembly of enzyme, alphabeta dimer
Y393N-alpha
-
no assembly of heterotetramer
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agriculture
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plants with enzymic activity show enhanced cold tolerance, role as a protective mechanism for growth of plants under sub optimal temperatures
medicine
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in patients with maple syrup urine disease, mutations such as R114W-alpha or R220W-alpha cause a strongly reduced binding of thiamin diphosphate, rendering the enzyme inactive
medicine
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naturally occuring mutations cause an impaired assembly of enzyme in patients with maple syrup urine disease
synthesis
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the enzyme is able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C-C bond formation, in particular for the enzymatic synthesis of diversely substituted 2-hydroxyketones with high enantioselectivity
synthesis
comparison of relevant properties for isobutanol production of Saccharomyces cerevisiae Aro10 and Lactococcus lactis KivD and KdcA genes. Activity in cell extracts reveals a superior Vmax/Km ratio of KdcA for alpha-ketoisovalerate and a wide range of linear and branched-chain 2-oxo acids. KdcA also shows the highest activity with pyruvate which, in engineered strains, can contribute to formation of ethanol as a by-product. During oxygen-limited incubation in the presence of glucose, strains expressing kdcA or kivD show a ca. twofold higher in vivo rate of conversion of alpha-ketoisovalerate into isobutanol than an Aro10-expressing strain. Cell extracts from cultures grown on different nitrogen sources reveal increased activity of constitutively expressed KdcA after growth on both valine and phenylalanine, while KivD and Aro10 activity is only increased after growth on phenylalanine
synthesis
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expression of branched-chain 2-oxoacid decarboxylase gene from Lactococcus lactis subsp. lactis CICC 6246 and alcohol dehydrogenase gene from Zymomonas mobilis CICC 41465 in Escherichia coli. Upon incubation in LB medium, much more 3-methyl-1-butanol (104 mg/l) than isobutanol (24 mg/l) is produced. In 5 g/l glucose-containing medium, 156 and 161 mg/l isobutanol and 3-methyl-1-butanol, respectively, is produced
synthesis
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use of the enzyme for catalytic asymmetric synthesis of (R)-phenylacetylcarbinol derivatives
synthesis
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expression of branched-chain 2-oxoacid decarboxylase gene from Lactococcus lactis subsp. lactis CICC 6246 and alcohol dehydrogenase gene from Zymomonas mobilis CICC 41465 in Escherichia coli. Upon incubation in LB medium, much more 3-methyl-1-butanol (104 mg/l) than isobutanol (24 mg/l) is produced. In 5 g/l glucose-containing medium, 156 and 161 mg/l isobutanol and 3-methyl-1-butanol, respectively, is produced
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synthesis
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comparison of relevant properties for isobutanol production of Saccharomyces cerevisiae Aro10 and Lactococcus lactis KivD and KdcA genes. Activity in cell extracts reveals a superior Vmax/Km ratio of KdcA for alpha-ketoisovalerate and a wide range of linear and branched-chain 2-oxo acids. KdcA also shows the highest activity with pyruvate which, in engineered strains, can contribute to formation of ethanol as a by-product. During oxygen-limited incubation in the presence of glucose, strains expressing kdcA or kivD show a ca. twofold higher in vivo rate of conversion of alpha-ketoisovalerate into isobutanol than an Aro10-expressing strain. Cell extracts from cultures grown on different nitrogen sources reveal increased activity of constitutively expressed KdcA after growth on both valine and phenylalanine, while KivD and Aro10 activity is only increased after growth on phenylalanine
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Wynn, R.M.; Davie, J.R.; Chuang, J.L.; Cote, C.D.; Chuang, D.T.
Impaired assembly of E1 decarboxylase of the branched-chain alpha-ketoacid dehydrogenase complex in type IA maple syrup urine disease
J. Biol. Chem.
273
13110-13118
1998
Homo sapiens
brenda
Oku, H.; Kaneda, T.
Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase
J. Biol. Chem.
263
18386-18396
1988
Bacillus subtilis
brenda
Kean, E.A.; Morrison, E.Y.St.A.
Isolation of a branched-chain alpha-keto acid decarboxylase from rat liver
Biochim. Biophys. Acta
567
12-17
1979
Rattus norvegicus
brenda
Chuang, J.L.; Wynn, R.M.; Song, J.L.; Chuang, D.T.
GroEL/GroES-dependent reconstitution of a2b2 tetramers of human mitochondrial branched chain alpha-ketoacid decarboxylase. Obligatory interaction of chaperonins with an alphabeta dimeric intermediate
J. Biol. Chem.
274
10395-10404
1999
Homo sapiens
brenda
Wang-Pruski, G.; Szalay, A.A.
Transfer and expression of the genes of Bacillus branched chain alpha-oxo acid decarboxylase in Lycopersicum esculentum
Electron. J. Biotechnol.
5
141-153
2002
Bacillus subtilis
-
brenda
Wynn, R.M.; Ho, R.; Chuang, J.L.; Chuang, D.T.
Roles of active site and novel K+ ion-binding site residues in human mitochondrial branched-chain alpha-ketoacid decarboxylase/dehydrogenase
J. Biol. Chem.
276
4168-4174
2001
Homo sapiens
brenda
Wynn, R.M.; Davie, J.R.; Cox, R.P.; Chuang, D.T.
Chaperonins GroEL and GroES promote assembly of heterotetramers (alpha2beta2) of mammalian mitochondrial branched-chain alpha-keto acid decarboxylase in Escherichia coli
J. Biol. Chem.
267
12400-12403
1992
Bos taurus, Homo sapiens
brenda
Davie, J.R.; Wynn, R.M.; Cox, R.P.; Chuang, D.T.
Expression and assembly of a functional E1 component (alpha2beta2) of mammalian branched-chain alpha-ketoacid dehydrogenase complex in Escherichia coli
J. Biol. Chem.
267
16601-16606
1992
Bos taurus, Homo sapiens
brenda
Li, J.; Wynn, R.M.; Machius, M.; Chuang, J.L.; Karthikeyan, S.; Tomchick, D.R.; Chuang, D.T.
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase
J. Biol. Chem.
279
32968-32978
2004
Homo sapiens
brenda
Smit, B.A.; van Hylckama Vlieg, J.E.; Engels, W.J.; Meijer, L.; Wouters, J.T.; Smit, G.
Identification, cloning, and characterization of a Lactococcus lactis branched-chain alpha-keto acid decarboxylase involved in flavor formation
Appl. Environ. Microbiol.
71
303-311
2005
Lactococcus lactis (Q6QBS4), Lactococcus lactis
brenda
de la Plaza, M.; Fernandez de Palencia, P.; Pelaez, C.; Requena, T.
Biochemical and molecular characterization of alpha-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
FEMS Microbiol. Lett.
238
367-374
2004
Lactococcus lactis subsp. lactis (Q684J7)
brenda
Berthold, C.L.; Gocke, D.; Wood, M.D.; Leeper, F.J.; Pohl, M.; Schneider, G.
Structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction
Acta Crystallogr. Sect. D
63
1217-1224
2007
Lactococcus lactis
brenda
Gocke, D.; Nguyen, C.L.; Pohl, M.; Stillger, T.; Walter, L.; Mueller, M.
Branched-chain keto acid decarboxylase from Lactococcus lactis (KdcA), a valuable thiamine diphosphate-dependent enzyme for asymmetric C-C bond formation
Adv. Synth. Catal.
349
1425-1435
2007
Lactococcus lactis
-
brenda
Werther, T.; Spinka, M.; Tittmann, K.; Schtz, A.; Golbik, R.; Mrestani-Klaus, C.; Hbner, G.; Knig, S.
Amino acids allosterically regulate the thiamine diphosphate-dependent alpha-keto acid decarboxylase from Mycobacterium tuberculosis
J. Biol. Chem.
283
5344-5354
2008
Mycobacterium tuberculosis (P9WG37), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WG37), Mycobacterium tuberculosis H37Rv
brenda
Atsumi, S.; Li, Z.; Liao, J.C.
Acetolactate synthase from Bacillus subtilis serves as a 2-ketoisovalerate decarboxylase for isobutanol biosynthesis in Escherichia coli
Appl. Environ. Microbiol.
75
6306-6311
2009
Bacillus subtilis (Q04789), Bacillus subtilis 168 (Q04789)
brenda
Islam, M.M.; Nautiyal, M.; Wynn, R.M.; Mobley, J.A.; Chuang, D.T.; Hutson, S.M.
The branched chain amino acid (BCAA) metabolon: Interaction of glutamate dehydrogenase with the mitochondrial branched chain aminotransferase (BCATm)
J. Biol. Chem.
285
265-276
2010
Rattus norvegicus
brenda
Savrasova, E.; Kivero, A.; Shakulov, R.; Stoynova, N.
Use of the valine biosynthetic pathway to convert glucose into isobutanol
J. Ind. Microbiol. Biotechnol.
38
1287-1294
2011
Lactococcus lactis
brenda
Wei, J.; Timler, J.G.; Knutson, C.M.; Barney, B.M.
Branched-chain 2-keto acid decarboxylases derived from Psychrobacter
FEMS Microbiol. Lett.
346
105-112
2013
Lactococcus lactis, Psychrobacter cryohalolentis, Psychrobacter arcticus, Psychrobacter cryohalolentis K5, Psychrobacter arcticus 273-4
brenda
Milne, N.; Van Maris, A.; Pronk, J.; Daran, J.
Comparative assessment of native and heterologous 2-oxo acid decarboxylases for application in isobutanol production by Saccharomyces cerevisiae
Biotechnol. Biofuels
8
204
2015
Lactococcus lactis (Q6QBS4), Lactococcus lactis B1157 (Q6QBS4)
brenda
Dickinson, J.R.; Lanterman, M.M.; Danner, D.J.; Pearson, B.M.; Sanz, P.; Harrison, S.J.; Hewlins, M.J.
A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae
J. Biol. Chem.
272
26871-26878
1997
Saccharomyces cerevisiae (Q07471), Saccharomyces cerevisiae
brenda
Dickinson, J.R.; Harrison, S.J.; Dickinson, J.A.; Hewlins, M.J.
An investigation of the metabolism of isoleucine to active amyl alcohol in Saccharomyces cerevisiae
J. Biol. Chem.
275
10937-10942
2000
Saccharomyces cerevisiae (Q07471), Saccharomyces cerevisiae
brenda
Beigi, M.; Gauchenova, E.; Walter, L.; Waltzer, S.; Bonina, F.; Stillger, T.; Rother, D.; Pohl, M.; Mueller, M.
Regio- and stereoselective aliphatic-aromatic cross-benzoin reaction enzymatic divergent catalysis
Chemistry
22
13999-14005
2016
Lactococcus lactis
brenda
Sutiono, S.; Carsten, J.; Sieber, V.
Structure-guided engineering of alpha-keto acid decarboxylase for the production of higher alcohols at elevated temperature
ChemSusChem
11
3335-3344
2018
Lactococcus lactis (Q6QBS4)
brenda
Heath, C.; Jeffries, A.; Hough, D.; Danson, M.
Discovery of the catalytic function of a putative 2-oxoacid dehydrogenase multienzyme complex in the thermophilic archaeon Thermoplasma acidophilum
FEBS Lett.
577
523-527
2004
Thermoplasma acidophilum (Q9HIA4 AND Q9HIA3)
brenda
Chen, X.; Xu, J.; Yang, L.; Yuan, Z.; Xiao, S.; Zhang, Y.; Liang, C.; He, M.; Guo, Y.
Production of C4 and C5 branched-chain alcohols by engineered Escherichia coli
J. Ind. Microbiol. Biotechnol.
42
1473-1479
2015
Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis CICC 6246
brenda