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Enzyme Nomenclature
Information on EC 4.1.1.72 - branched-chain-2-oxoacid decarboxylase
for references in articles please use BRENDA:EC4.1.1.72
Word Map on EC 4.1.1.72
- 4.1.1.72
-
alpha-ketoacid
-
syrup
-
maple
- alpha-ketoisocaproate
- acidosis
-
ketoacids
-
cheese
- e1alpha
- alpha-ketoisovalerate
-
minigene
-
bckas
-
dihydrolipoyl
- alpha-keto-beta-methylvalerate
-
transacylase
- medicine
- synthesis
- agriculture
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
4.1.1.72
-
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RECOMMENDED NAME
GeneOntology No.
branched-chain-2-oxoacid 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
-
-
-
(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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
simultaneous expression of human alpha-subunit and bovine beta-subunit of enzyme in Escherichia coli
-
-
simultaneous expression of human alpha-subunit and bovine beta-subunit of enzyme in Escherichia coli
-
-
enzyme may be a component of an enzyme complex named alpha-ketoisocaproate:alpha-keto-beta-methylvalerate dehydrogenase
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
pyruvate decarboxylase-like enzyme YDL080c appears to be the major route of decarboxylation of alpha-ketoisocaproate to isoamyl alcohol although at least one other unidentified decarboxylase can substitute to a minor extent
physiological function
-
metabolic routes between isoleucine and active amyl alcohol all involve the initial decarboxylation of isoleucine to 2-oxo-3-methylvalerate and subsequent decarboxylation to 2-methylbutanoate. One of the decarboxylases encoded by PDC1, PDC5, PDC6, YDL080c, or YDR380w must be present to allow yeast to utilize 2-oxo-3-methylvalerate. Any one of this family of decarboxylases is sufficient to allow the catabolism of isoleucine to active amyl alcohol; metabolic routes between isoleucine and active amyl alcohol all involve the initial decarboxylation of isoleucine to 2-oxo-3-methylvalerate and subsequent decarboxylation to 2-methylbutanoate. One of the decarboxylases encoded by PDC1, PDC5, PDC6, YDL080c, or YDR380w must be present to allow yeast to utilize 2-oxo-3-methylvalerate. Any one of this family of decarboxylases is sufficient to allow the catabolism of isoleucine to active amyl alcohol. In leucine catabolism, the enzyme encoded by YDL080c is solely responsible for the decarboxylation of alpha-ketoisocaproate, whereas in valine catabolism any one of the isozymes of pyruvate decarboxylase will decarboxylate 2-oxoisovalerate
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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
-
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
-
at 30 mM 1.2% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
3-(4-hydroxyphenyl)-2-oxopropanoic acid
(4-hydroxyphenyl)-acetaldehyde + CO2
-
at 30 mM 6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
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-methyl-2-oxohexanoic acid
3-methylpentanal + CO2
-
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
?
-
at 1 mM 0.85% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
oxo(phenyl)acetic acid
benzaldehyde + CO2
-
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
-
-
-
?
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
isobutanal + 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-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-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-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
-
-
-
?
L-3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
-
stereospecificity towards the L-isomer
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
8.8% of the activity with 2-oxoisovalerate
-
?
pyruvate
ethanal + CO2
-
25% of the activity with L-3-methyl-2-oxopentanoate
-
-
-
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
?
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
-
-
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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INHIBITORS
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
-
additional information
stopped-flow kinetics show that MtKDC is allosterically activated by 2-oxoacids, also amino acids are potent activators
-
additional information
-
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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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
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
0.05
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant D295A, pH 7.5, 30°C, overall reaction; wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; wild-type, 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
0.337
2-oxoisovalerate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.0066
thiamine diphosphate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.016
thiamine diphosphate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.026
thiamine diphosphate
-
mutant R301A, pH 7.5, 30°C, overall reaction; 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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
2-oxoisovalerate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; wild-type, pH 7.5, 30°C, overall reaction
0.38
2-oxoisovalerate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant Y300A, pH 7.5, 30°C, overall reaction
0.41
2-oxoisovalerate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant R301A, pH 7.5, 30°C, overall reaction
0.48
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant D295A, pH 7.5, 30°C, overall reaction
0.57
2-oxoisovalerate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant Y300F, pH 7.5, 30°C, overall reaction
0.8
2-oxoisovalerate
mutant Q487G, pH 7.0, 37°C; mutant Q487S, pH 7.0, 37°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
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
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
0.19
thiamine diphosphate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; wild-type, pH 7.5, 30°C, overall reaction
0.31
thiamine diphosphate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant Y300A, pH 7.5, 30°C, overall reaction
0.41
thiamine diphosphate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant R301A, pH 7.5, 30°C, overall reaction
0.42
thiamine diphosphate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant D295A, pH 7.5, 30°C, overall reaction
0.53
thiamine diphosphate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction; mutant Y300F, pH 7.5, 30°C, overall reaction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
2-oxoisovalerate
mutant Q487G, pH 7.0, 37°C; mutant Q487S, pH 7.0, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
124
pyruvate
weak substrate inhibition is detected for pyruvate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6: about 60% of maximum activity, pH 9: about 55% of maximum activity
6 - 7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
BCKDC proteins in the metabolon are found in all tissues except skeletal muscle, which harbors only the five subunits
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
37800
-
2 * 45500, alpha subunit, + 2 * 37800, beta subunit, SDS-PAGE, enzyme forms part of the branched chain alpha-ketoacid dehydrogenase complex
45000
45500
-
2 * 45500, alpha subunit, + 2 * 37800, beta subunit, SDS-PAGE, enzyme forms part of the branched chain alpha-ketoacid dehydrogenase complex
55000
160000
171000
-
with His6-tagged alpha subunits, gel filtration, sucrose density gradient
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
tetramer
additional information
tetramer
-
2 * 45500, alpha subunit, + 2 * 37800, beta subunit, SDS-PAGE, enzyme forms part of the branched chain alpha-ketoacid dehydrogenase complex
additional information
-
assembly of tetramer is promoted by chaperonins groEL and groES
additional information
-
concurrent expression of subunits alpha and beta is important for assembly
additional information
-
assembly of tetramer is promoted by chaperonins groEL and groES
additional information
-
concurrent expression of subunits alpha and beta is important for assembly
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
when the E1alpha subunit is fully phosphorylated, overall BCKDC activity is zero
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 25-26% (v/v) PEG 200 in 0.1 M MES buffer pH 6.2 as a precipitant
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
sufficiently stable up to 40°C, but rapidly loses activity at higher temperatures
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
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completely stable in the presence of 20% (v/v) DMSO (half-life: 150 h)
polyethyleneglycol
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rapidly inactivated in the presence of 15% (v/v) PEG-400
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel-charged metal chelating column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli Rosetta 2 (DE3) and various Escherichia coli strains
expression in Saccharomyces cerevisiae, in a decarboxylase-negative pdc1Delta,pdc5Delta, pdc6Delta, aro10Delta background
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
N222S-alpha
R114W-alpha
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naturally occuring mutation in maple syrup disease patients, strongly reduced binding of thiamin diphosphate, enzyme inactive
R220W-alpha
T166M-alpha
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enzyme inactive, with attenuated ability to bind thiamin diphosphate
Y368C-alpha
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slow assembly of enzyme as alphabeta dimer and alpha2beta2 tetramer
Y393N-alpha
R220W-alpha
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naturally occuring mutation in maple syrup disease patients, strongly reduced binding of thiamin diphosphate, enzyme inactive
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
after denaturation in 8 M urea, reconstitution at 23°C with absolute requirement of chaperonins GroEL/GroES and MgATP2-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
synthesis
medicine
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naturally occuring mutations cause an impaired assembly of enzyme in patients with maple syrup urine disease
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
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
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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
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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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.72)
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