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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
- syrup
-
maple
- alpha-ketoisocaproate
- acidosis
-
ketoacids
-
cheese
- alpha-ketoisovalerate
- e1alpha
-
bckas
-
transacylase
- synthesis
- alpha-keto-beta-methylvalerate
-
dihydrolipoyl
- medicine
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-keto acid decarboxylase, AlsS, BCKA, BCKAD, BCKDC, branched-chain 2-keto acid decarboxylase, branched-chain 2-oxoacid decarboxylase, branched-chain alpha-keto acid decarboxylase, branched-chain alpha-ketoacid dehydrogenase complex, branched-chain keto 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
-
-
-
-
branched-chain alpha-keto acid decarboxylase
-
-
-
-
branched-chain alpha-ketoacid dehydrogenase complex
-
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
-
-
-
-
decarboxylase, branched-chain oxo acid
-
-
-
-
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
-
-
-
(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 SOURCE
PATHWAYS
BRENDA
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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
-
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
-
-
?
3,5-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
-
-
-
-
?
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
?
-
-
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
-
-
?
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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
?
-
-
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
-
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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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
0.05
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.05
2-oxoisovalerate
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation 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
2.6
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/I404C, 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
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
14.6
3-methyl-2-oxobutanoate
mutant V461I/A290M/Q252N/D306G/E316R/F388Y, pH 6.5, 30°C
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
0.028
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
0.38
2-oxoisovalerate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.41
2-oxoisovalerate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.48
2-oxoisovalerate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.57
2-oxoisovalerate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
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
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
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
0.31
thiamine diphosphate
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.41
thiamine diphosphate
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.42
thiamine diphosphate
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.53
thiamine diphosphate
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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 - 7
6 - 9
-
pH 6: about 60% of maximum activity, pH 9: about 55% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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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
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simultaneous expression of human alpha-subunit and bovine beta-subunit of enzyme in Escherichia coli
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enzyme may be a component of an enzyme complex named alpha-ketoisocaproate:alpha-keto-beta-methylvalerate dehydrogenase
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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BCKDC proteins in the metabolon are found in all tissues except skeletal muscle, which harbors only the five subunits
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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. 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
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
Show AA Sequence and Transmembrane Helices (106 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
171000
-
with His6-tagged alpha subunits, gel filtration, sucrose density gradient
37000
37800
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2 * 45500, alpha subunit, + 2 * 37800, beta subunit, SDS-PAGE, enzyme forms part of the branched chain alpha-ketoacid dehydrogenase complex
45000
45500
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2 * 45500, alpha subunit, + 2 * 37800, beta subunit, SDS-PAGE, enzyme forms part of the branched chain alpha-ketoacid dehydrogenase complex
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
tetramer
additional information
tetramer
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2 * 45500, alpha subunit, + 2 * 37800, beta subunit, SDS-PAGE, enzyme forms part of the branched chain alpha-ketoacid dehydrogenase complex
additional information
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assembly of tetramer is promoted by chaperonins groEL and groES
additional information
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concurrent expression of subunits alpha and beta is important for assembly
additional information
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assembly of tetramer is promoted by chaperonins groEL and groES
additional information
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concurrent expression of subunits alpha and beta is important for assembly
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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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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PROTEIN VARIANTS
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
V461I
3.3 degrees 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
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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sufficiently stable up to 40°C, but rapidly loses activity at higher temperatures
70.5
mutant V461I/A290M/Q252N/D306G/E316R/F388Y, melting temperature
74.5
75.5
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/I404C, melting temperature
74.5
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C, melting temperature
74.5
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290C, melting temperature
74.5
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290V, melting temperature
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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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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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.; Schütz, A.; Golbik, R.; Mrestani-Klaus, C.; Hübner, G.; König, 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
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