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Information on EC 4.1.1.72 - branched-chain-2-oxoacid decarboxylase
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4.1.1.72 branched-chain-2-oxoacid decarboxylaseIUBMB Comments
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.
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Word Map
- 4.1.1.72
-
alpha-ketoacid
-
maple
- syrup
- acidosis
- alpha-ketoisocaproate
-
ketoacids
-
cheese
- alpha-ketoisovalerate
- e1alpha
-
bckas
-
dihydrolipoyl
-
transacylase
- alpha-keto-beta-methylvalerate
- synthesis
- medicine
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bckad, ydl080c, alpha-keto acid decarboxylase, branched-chain alpha-keto acid decarboxylase, branched-chain 2-keto acid decarboxylase, branched-chain keto acid decarboxylase, mtkdc, branched-chain oxo acid decarboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-keto acid decarboxylase
AlsS
BCKA
-
-
-
-
branched-chain 2-keto acid decarboxylase
branched-chain 2-oxoacid decarboxylase
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-
-
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branched-chain alpha-keto acid decarboxylase
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-
-
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branched-chain alpha-ketoacid dehydrogenase complex
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the protein complex also contains glutamate dehydrogenase 1, 4-nitrophenylphosphatase domain and non-neuronal SNAP25-like protein homolog 1, pyruvate carboxylase, and BCKDC kinase
branched-chain keto acid decarboxylase
branched-chain oxo acid decarboxylase
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-
-
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decarboxylase, branched-chain oxo acid
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-
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KDC
KdcA
MtKDC
branched-chain keto acid decarboxylase
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2
acts on a number of 2-oxo acids, with a high affinity toward branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids
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-
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(3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2
binding of cofactor thiamine diphosphate to E1b component of enzyme induces a disorder-to-order transition of the conserved phosphorylation loop carrying phosphorylation sites S292 and S302
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(3S)-3-methyl-2-oxopentanoate carboxy-lyase (2-methylbutanal-forming)
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.
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CAS REGISTRY NUMBER
COMMENTARY
63653-19-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-oxoglutarate
CO2 + succinate semialdehyde
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5% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
2-oxoisopentanoate
CO2 + isobutanal
-
63% of the activity with L-3-methyl-
-
-
?
2-oxopropanoic acid
acetaldehyde + CO2
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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
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at 30 mM 6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
3-formylbenzonitrile + 2-oxobutanoic acid
3-[(1R)-1-hydroxy-2-oxobutyl]benzonitrile
-
-
-
-
?
4-(4-hydroxyphenyl)-2-oxobutanoic acid
3-(4-hydroxyphenyl)-propanal + CO2
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at 30 mM 1.6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-(methylsulfanyl)-2-oxobutanoic acid
3-(methylsulfanyl)-propanal + CO2
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at 30 mM 18% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-methyl-2-oxohexanoic acid
3-methylpentanal + CO2
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at 30 mM 19% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
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
-
-
?
indole-3-pyruvate
?
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at 1 mM 0.85% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
oxo(phenyl)acetic acid
benzaldehyde + CO2
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at 30 mM 8.4% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
(indol-3-yl)pyruvate
(indol-3-yl)acetaldehyde + CO2
-
-
-
?
(indol-3-yl)pyruvate
(indol-3-yl)acetaldehyde + CO2
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-
-
?
2-oxobutanoic acid
propanal + CO2
10% of the rate with 3-methyl-2-oxobutanoic acid
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-
?
2-oxobutanoic acid
propanal + CO2
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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
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-
?
2-oxohexanoic acid
pentanal + CO2
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at 30 mM 13% activity relative to 3-methyl-2-oxobutanoic acid
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-
?
2-oxoisocaproate
3-methylbutanal + CO2
22.7% of the activity with 2-oxoisovalerate
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-
?
2-oxoisohexanoate
CO2 + isopentanal
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38% of the activity with L-3-methyl-2-oxopentanoate
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?
2-oxoisohexanoate
CO2 + isopentanal
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38% of the activity with L-3-methyl-2-oxopentanoate
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-
?
2-oxomethylvalerate
pentanal + CO2
16.7% of the activity with 2-oxoisovalerate
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-
?
2-oxopentanoic acid
butanal + CO2
25% of the rate with 3-methyl-2-oxobutanoic acid
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?
2-oxopentanoic acid
butanal + CO2
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at 30 mM 15% activity relative to 3-methyl-2-oxobutanoic acid
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-
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
30% of the rate with 3-methyl-2-oxobutanoic acid
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-
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
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at 30 mM 38.1% activity relative to 3-methyl-2-oxobutanoic acid
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-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
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-
-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
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-
-
?
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
35% of the rate with 3-methyl-2-oxobutanoic acid
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-
?
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
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at 30 mM 26.3% activity relative to 3-methyl-2-oxobutanoic acid
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-
?
4-methylthio-2-oxobutanoate
3-methylthiopropanal + CO2
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-
-
?
L-3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
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stereospecificity towards the L-isomer
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-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
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8.8% of the activity with 2-oxoisovalerate
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?
pyruvate
ethanal + CO2
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25% of the activity with L-3-methyl-2-oxopentanoate
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?
additional information
?
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essential for the synthesis of branched-chain fatty acids
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?
additional information
?
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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
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?
additional information
?
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acetolactate synthase AlsS, EC 2.2.1.6, is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro
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?
additional information
?
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acetolactate synthase AlsS, EC 2.2.1.6, is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro
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?
additional information
?
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3-fluoro-2-oxopropanoic acid, isobutyraldehyde, 3,5-dichlorobenzaldehyde, 3,5-dimethoxybenzaldehyde and 2-oxooctanoic acid are no substrates
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?
additional information
?
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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
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?
additional information
?
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enzyme additionallly catalyzes the asymmetric synthesis of chiral 2-hydroxy ketones with high stereochemical purity
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?
additional information
?
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very poor substrates: indole-3-pyruvate and pyruvate
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
enzyme is a non-oxidative thiamin diphosphate-dependent alpha-oxoacid decarboxylase
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxymercuribenzoic acid
1 mM, 59% residual activity
phenylmethanesulfonyl fluoride
1 mM, 71.7% residual activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
stopped-flow kinetics show that MtKDC is allosterically activated by 2-oxoacids, also amino acids are potent activators
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additional information
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stopped-flow kinetics show that MtKDC is allosterically activated by 2-oxoacids, also amino acids are potent activators
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additional information
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GDH1 alone does not have a significant effect on BCKDC activity. However, addition of GDH1 and glutamate enhance the calculated kcat value by 40-45% with mitochondrial branched-chain aminotransferase present when compared with BCKDC plus branched-chain alpha-keto acids alone
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
0.264
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