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2 pyruvate
(S)-acetolactate + CO2
2-keto-4-methylhexanoic acid
3-methylpentanal + CO2
-
-
-
?
2-ketobutanoic acid
propanal + CO2
-
-
-
?
2-ketobutyrate
?
lower activity than with pyruvate
-
?
2-ketobutyric acid
propanal + CO2
-
-
-
-
?
2-ketohexanoic acid
pentanal + CO2
-
-
-
?
2-ketopentanoic acid
butanal + CO2
-
-
-
?
2-ketovalerate
?
lower activity than with pyruvate
-
?
2-oxo-4-methylpentanoate
3-methylbutanaldehyde + CO2
-
-
-
?
2-oxo-4-methylpentanoate
?
2-oxo-4-phenylbutanoic acid
3-phenylpropanal + CO2
-
-
-
-
?
2-oxo-4-phenylbutanoic acid
?
2-oxo-5-phenylpentanoic acid
4-phenylbutanal + CO2
-
-
-
-
?
2-oxo-5-phenylpentanoic acid
?
2-oxobutanoate
propionaldehyde + CO2
2-oxobutanoic acid
propanal + CO2
-
-
-
-
?
2-oxohexanoic acid
n-pentanal + CO2
-
-
-
-
?
2-oxohexanoic acid
pentanal + CO2
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
2-Oxoisopentanoate
?
-
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
2-oxomethylvalerate
?
16.7% of the activity with 2-oxoisovalerate
-
-
?
2-oxomethylvalerate
pentanal + CO2
-
-
-
?
2-oxooctanoic acid
?
-
-
-
-
?
2-oxooctanoic acid
n-hexanal + CO2
-
-
-
-
?
2-oxopentanoate
butanaldehyde + CO2
-
-
-
?
2-oxopentanoate
butyraldehyde + CO2
2-oxopentanoic acid
butanal + CO2
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
2-oxopentanoic acid
n-butanal + CO2
-
-
-
-
?
3-(1H-indol-3-yl)-2-oxopropanoic acid
1H-indol-3-ylacetaldehyde + CO2
-
-
-
-
?
3-(1H-indol-3-yl)-2-oxopropanoic acid
?
-
-
-
-
?
3-fluoro-2-oxopropanoic acid
?
-
-
-
-
?
3-fluoro-2-oxopropanoic acid
fluoroacetaldehyde + CO2
-
-
-
-
?
3-Fluoropyruvate
acetate + F- + CO2
3-Hydroxypyruvate
Glycolaldehyde + CO2
3-methyl-2-oxobutanoate
?
-
-
-
-
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
-
-
-
-
?
3-methyl-2-oxopentanoic acid
?
3-phenyl-2-oxopropanoate
?
-
-
-
?
3-phenylpyruvate
2-phenylethanal + CO2
8.8% of the activity with 2-oxoisovalerate
-
-
?
4-hydroxyphenylpyruvate
?
-
-
-
-
?
4-methyl-2-oxohexanoic acid
3-methylpentanal + CO2
-
-
-
-
?
4-methyl-2-oxohexanoic acid
?
4-methyl-2-oxopentanoate
?
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
-
-
-
-
?
4-methyl-2-oxopentanoic acid
?
-
-
-
-
?
4-methylthio-2-oxobutanoate
3-methylthiopropanal + CO2
7.2% of the activity with 2-oxoisovalerate
-
-
?
a 2-oxo acid
an aldehyde + CO2
-
-
-
-
?
acetaldehyde + acetaldehyde
(S)-acetoin + ?
acetaldehyde + acetaldehyde
acetoin
acetaldehyde + benzaldehyde
(1R)-phenylacetylcarbinol
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
acetylphosphinate
?
-
-
-
-
?
benzaldehyde + acetaldehyde
(R)-phenylacetylcarbinol
-
-
reaction proceeds under in vitro assay conditions, colorimetric assay based on reaction
-
?
benzaldehyde + pyruvate
(1R)-phenylacetylcarbinol + CO2
-
-
-
-
ir
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
-
-
transformation is enhanced by maintenance of neutral pH-value
-
?
benzaldehyde + pyruvate
L-phenylacetylcarbinol + CO2
-
-
-
-
?
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
benzoylformate
benzaldehyde + CO2
substrate only for mutant mutant I472A
-
-
?
beta-hydroxypyruvate
2,4-dihydroxymethyl-3-oxo-butanoic acid
-
D28A YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
beta-hydroxypyruvate
glycolaldehyde + ?
-
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
1,3,4-trihydroxy-2-butanone
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
cinnamaldehyde
(2S,3R)-5-phenylpent-4-ene-2,3-diol + CO2
indole-3-pyruvate
2-(indol-3-yl)-ethanal + CO2
0.1% of the activity with 2-oxoisovalerate
-
-
?
oxo(phenyl)acetic acid
?
-
-
-
-
?
oxo(phenyl)acetic acid
benzaldehyde + CO2
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
pyruvate
acetaldehyde + CO2
pyruvate + acetaldehyde
acetoin + CO2
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
pyruvate + CoA + 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
-
-
?
pyruvate + phenylacetaldehyde
3-hydroxy-4-phenyl-butan-2-one + CO2
enzyme catalyzes a carboligation as side reaction
-
?
pyruvic acid
acetaldehyde + CO2
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
additional information
?
-
2 pyruvate
(S)-acetolactate + CO2
-
-
-
?
2 pyruvate
(S)-acetolactate + CO2
-
D28A YPDC variant, not E477Q YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
2-oxo-4-methylpentanoate
?
-
-
-
?
2-oxo-4-methylpentanoate
?
-
-
-
?
2-oxo-4-methylpentanoate
?
-
-
-
-
?
2-oxo-4-methylpentanoate
?
-
-
-
-
?
2-oxo-4-phenylbutanoic acid
?
-
-
-
-
?
2-oxo-4-phenylbutanoic acid
?
-
-
-
-
?
2-oxo-5-phenylpentanoic acid
?
-
-
-
-
?
2-oxo-5-phenylpentanoic acid
?
-
-
-
-
?
2-Oxobutanoate
?
-
-
-
?
2-Oxobutanoate
?
-
-
-
-
?
2-Oxobutanoate
?
-
-
-
-
?
2-Oxobutanoate
?
-
-
-
-
?
2-oxobutanoate
propionaldehyde + CO2
-
-
-
?
2-oxobutanoate
propionaldehyde + CO2
-
-
-
-
?
2-oxobutanoate
propionaldehyde + CO2
-
-
-
-
?
2-oxobutanoic acid
?
-
-
-
-
?
2-oxobutanoic acid
?
-
-
-
-
?
2-oxohexanoic acid
?
-
-
-
-
?
2-oxohexanoic acid
?
-
-
-
-
?
2-oxohexanoic acid
?
-
-
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
22.7% of the activity with 2-oxoisovalerate
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
-
-
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
-
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
-
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
-
-
-
-
?
2-Oxopentanoate
?
-
-
-
?
2-Oxopentanoate
?
-
-
-
?
2-Oxopentanoate
?
-
-
-
-
?
2-Oxopentanoate
?
-
-
-
-
?
2-Oxopentanoate
?
-
-
-
-
?
2-oxopentanoate
butyraldehyde + CO2
-
-
-
-
?
2-oxopentanoate
butyraldehyde + CO2
-
-
-
-
?
2-oxopentanoic acid
?
-
-
-
-
?
2-oxopentanoic acid
?
-
-
-
-
?
3-Fluoropyruvate
acetate + F- + CO2
-
decarboxylation is followed by release of F-
-
?
3-Fluoropyruvate
acetate + F- + CO2
-
decarboxylation is followed by release of F-
-
?
3-Hydroxypyruvate
Glycolaldehyde + CO2
-
-
-
?
3-Hydroxypyruvate
Glycolaldehyde + CO2
-
-
-
-
?
3-methyl-2-oxopentanoic acid
?
-
-
-
-
?
3-methyl-2-oxopentanoic acid
?
-
-
-
-
?
4-methyl-2-oxohexanoic acid
?
-
-
-
-
?
4-methyl-2-oxohexanoic acid
?
-
-
-
-
?
4-methyl-2-oxopentanoate
?
-
-
-
-
?
4-methyl-2-oxopentanoate
?
-
-
-
-
?
acetaldehyde + acetaldehyde
(S)-acetoin + ?
-
-
-
-
?
acetaldehyde + acetaldehyde
(S)-acetoin + ?
-
-
-
-
?
acetaldehyde + acetaldehyde
(S)-acetoin + ?
-
-
-
-
?
acetaldehyde + acetaldehyde
acetoin
-
carboligation of 2 aldehydes as a side reaction of PDC
-
?
acetaldehyde + acetaldehyde
acetoin
-
carboligation of 2 aldehydes as a side reaction of PDC
-
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
carboligation of 2 aldehydes as a side reaction of PDC, high carboligase activity, more active than PDC from Zymomonas mobilis
(R)-phenylacetylcarbinol
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
carboligation of 2 aldehydes as a side reaction of PDC, less active than PDC from Saccharomyces cerevisiae
(R)-phenylacetylcarbinol
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
-
-
-
?
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
-
-
-
-
ir
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
-
-
-
-
ir
cinnamaldehyde
(2S,3R)-5-phenylpent-4-ene-2,3-diol + CO2
-
-
-
-
?
cinnamaldehyde
(2S,3R)-5-phenylpent-4-ene-2,3-diol + CO2
-
-
-
-
?
Phenylpyruvate
?
-
-
-
-
?
Phenylpyruvate
?
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
?
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
enzyme catalyzes a carboligation as side reaction
-
?
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
enzyme catalyzes a carboligation as side reaction
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
ethanol fermentation pathway, involved in anaerobic metabolism
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
Citrus sp.
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, contains catalytic and regulatory pyruvate binding site
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
pyruvate
acetaldehyde + CO2
catalytic cycle, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, contains catalytic and regulatory pyruvate binding site
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
Pdc is involved in the operation of ethanolic fermentation pathway that appears to correlate to an extent with anoxia tolerance in plants, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80°C (pH 8.0), the apparent Vm value for pyruvate decarboxylation is about 40% of the apparent Vm value for pyruvate oxidation rate (using Pyrococcus furiosus ferredoxin as the electron acceptor), 60% at pH 10.2 (80°C)
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
plus acetoin
?
pyruvate
acetaldehyde + CO2
-
-
plus acetoin
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
-
-
r
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
3-4% acetoin side product
?
pyruvate
acetaldehyde + CO2
-
mechanism
-
ir
pyruvate
acetaldehyde + CO2
-
mechanism
-
ir
pyruvate
acetaldehyde + CO2
-
catalytic mechanism
-
ir
pyruvate
acetaldehyde + CO2
-
4 active sites in the tetramer, enzyme structure
-
?
pyruvate
acetaldehyde + CO2
-
alternating sites mechanism
-
?
pyruvate
acetaldehyde + CO2
-
catalytic cycle, 3 domains: a diphosphate-binding domain, a pyrimidine-binding domain and a regulatory domain, model for enzyme regulation
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, acetaldehyde is produced by protonation of the key C2alpha-carbanion/enamine intermediate
-
ir
pyruvate
acetaldehyde + CO2
-
detailed mechanism
-
ir
pyruvate
acetaldehyde + CO2
-
detailed mechanism with roles for the active center acid-base groups D28, E477, H114 and H115, catalytic cycle, mechanistic model of the reaction, alternating sites model
-
ir
pyruvate
acetaldehyde + CO2
-
detailed mechanism, catalytic cycle, alternating sites mechanism based on tight communication between active sites of the functional dimer, with the ionizable residues D28, E477 and H115 likely to be important in creating this communication, enzyme exists in three conformations, one inactive and two active forms, enzyme structure
-
ir
pyruvate
acetaldehyde + CO2
-
nonoxidative decarboxylation, main reaction
-
?
pyruvate
acetaldehyde + CO2
-
enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
key role in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step of alcohol fermentation
-
ir
pyruvate
acetaldehyde + CO2
-
regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
-
-
?
pyruvate
acetaldehyde + CO2
catalytic cycle, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
4 active sites in the tetramer, enzyme structure
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
only the undissociated pyruvic acid acts as the substrate
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
nonoxidative decarboxylation
-
?
pyruvate
acetaldehyde + CO2
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
nonoxidative decarboxylation
-
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
in wild-type, about 10% of the acetolactate forming activity
-
?
pyruvate
acetaldehyde + CO2
-
in wild-type, about 10% of the acetolactate forming activity
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
plus racemic acetoin
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
involved in the enhancement of ethanol production in berries, but not the limiting factor
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
first enzyme in a branch of glycolysis that converts pyruvate to ethanol
?
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
key enzyme in alcoholic fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
key enzyme in alcoholic fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
active site structure, catalytic mechanism
-
?
pyruvate
acetaldehyde + CO2
C-terminal region occludes the active site, enzyme structure, catalytic cycle, active site closure is required for decarboxylation
-
?
pyruvate
acetaldehyde + CO2
-
H113 is involved in substrate binding and mediates the opening and closing of the active site by ion pairing with the carboxyl group of pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
nonoxidative decarboxylation, main reaction
-
?
pyruvate
acetaldehyde + CO2
-
catalyzes the penultimate step in ethanol fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
ethanal + CO2
0.6% of the activity with 2-oxoisovalerate
-
-
?
pyruvate
ethanal + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
i.e. 3-hydroxy-2-butanone, formation of the (R)- and the (S)-enantiomers
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
carboligation reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
carboligation reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
wild-type 100% conversion, 98% enantiomeric excess, mutant I472A, 60% conversion, 70% enantiomeric excess, mutant I476E, 6% conversion, 60% enantiomeric excess of S-enantiomer
-
-
?
additional information
?
-
-
even with benzaldehyde as the only substrate no benzoin can be detected, the enzyme does not produce (S)-2-hydroxypropiophenone
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
involved in fruit ripening and aroma biogenesis
-
-
?
additional information
?
-
involved in fruit ripening and aroma biogenesis
-
-
?
additional information
?
-
-
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
?
additional information
?
-
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
?
additional information
?
-
no substrate: indole-3-pyruvate
-
-
?
additional information
?
-
no substrate: indole-3-pyruvate
-
-
?
additional information
?
-
-
no substrate: indole-3-pyruvate
-
-
?
additional information
?
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity with 3-phenyl-2-oxopropanoate, benzoyl formate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity with 3-phenyl-2-oxopropanoate, benzoyl formate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
isoform Pdc5p lacks enzymatic activity
-
-
?
additional information
?
-
-
isoform Pdc5p lacks enzymatic activity
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
substrate specificity of the engineered KdcA mutant enzymes with branched and unbranched 2-oxo acid substrates, overview
-
-
?
additional information
?
-
-
involved in aerobic fermentation in mature pollen
-
-
?
additional information
?
-
-
no activity is recorded on 3-phenyl-2-oxopropanoate, benzoylformate, 4-hydroxyphenylpyruvate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity is recorded on 3-phenyl-2-oxopropanoate, benzoylformate, 4-hydroxyphenylpyruvate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
critical enzyme in a pollen-specific pathway to bypass pyruvate dehydrogenase enzymes and maintain biosynthetic capacity and energy production under the unique conditions prevailing during pollen-pistil interaction
-
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
?
additional information
?
-
-
key enzyme in alcoholic fermentation
-
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
?
additional information
?
-
-
the role of the protein component of pyruvate decarboxylase in the mechanism of substrate activation
-
-
?
additional information
?
-
-
catalyzes also carboligase reactions in which the central enamine intermediate reacts with acetaldehyde or pyruvate, instead of the usual proton electrophile, resulting in the formation of acetoin and acetolactate, respectively, typically 1% of the total reaction, stereochemistry of products
-
?
additional information
?
-
-
enzyme catalyzes a carboligase reaction as side reaction forming acetoin and acetolactate
-
?
additional information
?
-
-
enzyme catalyzes also a carboligation as side reaction producing acetoin and acetolactate, mechanism, not: pyruvamide
-
?
additional information
?
-
-
not: pyruvamide
-
?
additional information
?
-
-
not: pyruvamide
-
?
additional information
?
-
-
oxidative diversion of the decarboxylation of pyruvate by 2,6-dichlorophenolindophenol, which traps a carbanionic intermediate and diverts the product from acetaldehyde to acetate, kinetics
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
in the pyruvamide-activated enzyme form, the flexible loop located on the beta-domain can transfer information to the active center thiamine diphosphate located at the interface of the alpha and gamma domains, overview
-
-
?
additional information
?
-
-
thiamine-dependent decarboxylases/dehydrogenases can also carry out socalled carboligation reactions, where the central ThDP-bound enamine intermediate reacts with electrophilic substrates, YPDC can produce acetoin and acetolactate, resulting from the reaction of the central thiamine diphosphate-bound enamine with acetaldehyde and pyruvate, respectively, overview, analysis of the stereoselectivity for forming the carboligase products acetoin, acetolactate, and phenylacetylcarbinol by the YPDC mutants E477Q and D28A
-
-
?
additional information
?
-
-
does not act on phenylpyruvate
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
enzymatic stereoselective synthesis of L-norephedrine by coupling recombinant R-selective pyruvate decarboxylase from from Saccharomyces cerevisiae and an S-selective omega-transaminase from Vibrio fluvialis JS17, method optimization, overview
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
one of the key enzymes involved in fermentation process
-
-
?
additional information
?
-
-
involved in a pathway in which NAD+ is regenerated under anaerobic conditions
-
-
?
additional information
?
-
nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
-
?
additional information
?
-
-
nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
-
?
additional information
?
-
nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
-
?
additional information
?
-
-
even with benzaldehyde as the only substrate no benzoin can be detected, the enzyme does not produce (S)-2-hydroxypropiophenone
-
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
?
additional information
?
-
-
key enzyme in glycolytic pathway to ethanol
-
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
?
additional information
?
-
PDC has no activity with benzoylformate
-
-
?
additional information
?
-
-
PDC has no activity with benzoylformate
-
-
?
additional information
?
-
-
pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a 2-oxo acid
an aldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
pyruvate + acetaldehyde
acetoin + CO2
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
additional information
?
-
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate
acetaldehyde + CO2
key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
ir
pyruvate
acetaldehyde + CO2
ethanol fermentation pathway, involved in anaerobic metabolism
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
Pdc is involved in the operation of ethanolic fermentation pathway that appears to correlate to an extent with anoxia tolerance in plants, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
ir
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
key role in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step of alcohol fermentation
-
ir
pyruvate
acetaldehyde + CO2
-
regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
involved in the enhancement of ethanol production in berries, but not the limiting factor
-
?
pyruvate
acetaldehyde + CO2
enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux
-
-
?
pyruvate
acetaldehyde + CO2
key enzyme in alcoholic fermentation
-
?
pyruvate
acetaldehyde + CO2
key enzyme in alcoholic fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
?
pyruvate
acetaldehyde + CO2
-
catalyzes the penultimate step in ethanol fermentation
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
involved in fruit ripening and aroma biogenesis
-
-
?
additional information
?
-
involved in fruit ripening and aroma biogenesis
-
-
?
additional information
?
-
-
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
?
additional information
?
-
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
involved in aerobic fermentation in mature pollen
-
-
?
additional information
?
-
-
critical enzyme in a pollen-specific pathway to bypass pyruvate dehydrogenase enzymes and maintain biosynthetic capacity and energy production under the unique conditions prevailing during pollen-pistil interaction
-
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
?
additional information
?
-
-
key enzyme in alcoholic fermentation
-
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
one of the key enzymes involved in fermentation process
-
-
?
additional information
?
-
-
involved in a pathway in which NAD+ is regenerated under anaerobic conditions
-
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
?
additional information
?
-
-
key enzyme in glycolytic pathway to ethanol
-
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
?
additional information
?
-
-
pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphoryldifluoromethyl)phosphonic acid
-
-
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphorylmethyl) phosphonic acid
-
-
1,10-phenanthroline
1 mM, 95% inhibition
2,6-dichlorophenolindophenol
-
0.1 mM, weak inhibition
2-Hydroxy-5-nitrobenzyl-dimethylsulfonium bromide
-
-
2-p-Toluidinonaphthalene-6-sulfonate
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethanol
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-5-methyl-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
a thiamine diphosphate analogue, almost irreversible inhibition
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
a methyl triazole analogue of thiamine diphosphate, almost irreversible inhibition
3-deazathiamine diphosphate
-
12-step synthesis of the isoelectronic thiophene analogue of thiamine diphosphate, overview
4-Methylpyrazole
-
competitive inhibitor
Ag+
complete inhibition at 20 mM
Cu+
complete inhibition at 20 mM
Cu2+
1 mM, 95% inhibition
ethylendiaminetetraacetate
1 mM, 95% inhibition
glyoxylate
complete inhibition
Guanidinium chloride
-
6 M, denaturates
Hg2+
-
0.15 mM, 50% inhibition
maleate buffer
inhibits at low pyruvate concentrations
mono(2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl) iminodiacetate
-
-
mono[2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl] malonate
-
-
N-([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]sulfonyl)phosphoramidic acid
-
-
O-2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl sulfamate
-
-
Omeprazole
-
50% inhibition at 0.016 mg/ml for enzyme from metronidazole-resistant strain or from cells grown under iron-limited conditions, little effect on enzyme from metronidazole-susceptible strain
p-hydroxymercuribenzoate
1 mM, 40% inhibition
phenylpyruvate
10 mM, 81% inhibition
phosphoramidon
1 mM, 48% inhibition
thiamine diphosphate
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)sulfonyl]phosphoramidic acid
-
a phosphoramidic acid thiamine diphosphate analogue
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl](difluoro)methyl]phosphonic acid
-
a difluoromethylenediphosphonate ester thiamine diphosphate analogue
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl]methyl]phosphonic acid
-
a methylenediphosphonate ester thiamine diphosphate analogue
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
-
reversible
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
-
-
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
-
wild type enzyme and mutant enzymes D28A, H114F, H115F and E477Q
3-hydroxypyruvate
-
competitive inhibitor
acetaldehyde
-
inhibits, more resistant than PDC from Zymomonas mobilis, 8 mM, 2h, stable
acetaldehyde
-
0.4 mM, inactivates
benzaldehyde
-
inhibits formation of (R)-1-phenyl-1-hydroxy-propane-2-one
benzaldehyde
-
after a 20 h incubation with 30 mM benzaldehyde, the residual activity is 84% of the initial activity, enzyme stability dramatically decreases in the presence of 200 mM benzaldehyde (27% residual activity after 3 h incubation)
glyoxalate
-
irreversible
glyoxalate
-
mechanism-based inhibitor
p-chloromercuribenzoate
-
reversed by dithiothreitol
p-chloromercuribenzoate
-
-
phosphate
-
-
phosphate
-
competitive inhibition
phosphate
-
poor inhibitor at high concentrations
Pyruvamide
-
mixed type inhibitor
Pyruvamide
-
inhibits at high concentrations
pyruvate
-
weak substrate inhibition, above 100 mM
pyruvate
substrate inhibition at pyruvate concentrations above 20 mM for isoenzyme 1; substrate inhibition at pyruvate concentrations above 40 mM for isoenzyme 2
pyruvate
-
substrate inhibition at high concentrations
pyruvate
-
modest substrate inhibition at high concentrations
pyruvate
substrate inhibition above 25 mM
Zn2+
1 mM, 35% inhibition
Zn2+
-
0.5 mM ZnCl2, 82% reduction of activity
additional information
-
no inhibition by ferredoxin
-
additional information
-
growth on a medium with oxythiamine increases enzyme activity, but may be in response to an earlier inhibition of enzyme leading to an accumulation of pyruvate, which induces the biosynthesis of enzyme apoform
-
additional information
-
dephosphorylation of Pdc1p by alkaline phosphatase inhibits the enzyme activity by 50%
-
additional information
not inhibited by 25 mM EGTA or EDTA, at 37°C, pH 6.5, 90 min, without cofactors
-
additional information
-
not inhibited by 25 mM EGTA or EDTA, at 37°C, pH 6.5, 90 min, without cofactors
-
additional information
-
no product inhibition by (R)-1-phenyl-1-hydroxy-propane-2-one
-
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chromate
-
sulfur starvation and chromate treatment induce the expression of Pdc6, PDC6 mRNA level is increased more than 100fold following chromate treatment with toxic doses (0.005, 0.01, and 0.02 mM) but remains unchanged at the lower dose 0.0025 mM
CO2
-
PDC activity increases when fruit is treated with 20% CO2 than when fruit is stored in air
Met32 protein
-
dependent upon Met32 protein
-
NaCl
up to 3fold increase in activity at pH 5.4
phosphatidylcholine
-
activates at 2 mg/ml
sodium bis(2-ethyl-1-hexyl)sulfosuccinate
-
a synthetic surfactant
Pyruvamide
-
artificial activator
Pyruvamide
the activator pyruvamide arrests the flexible loops comprising residues 106-113 and 292-301, so that two of four active sites become closed
Pyruvamide
-
activates, pyruvate and pyruvamide have different activation pathways with distinct binding sites
Pyruvamide
-
activation mechanism, binds only at the regulatory site, but with lower affinity than does pyruvate
Pyruvamide
-
activator, 2 binding sites per dimer, mode of binding, a disorder-order transition of two active-site loop regions is a key event in the activation process, kinetic data, mechanism
Pyruvamide
-
artificial activator
Pyruvamide
-
a substrate activator surrogate, activates, a flexible loop spanning residues 290 to 304 on the beta-domain of the enzyme, not seen in the absence of pyruvamide, occurs in presence of the activator, residues on the loop affect the enzyme activity, conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure
Pyruvamide
the activator pyruvamide arrests one of the flexible loops comprising residues 106-113 and 292-301, so that two of four active sites become closed, the loop of residues 105-113 remains flexible in the nonactivated enzyme, overview
pyruvate
-
concentration-dependent substrate activation, minimum at 1.5 mM, mechanism, kinetics
pyruvate
allosteric substrate activation, binding of substrate at a regulatory site induces catalytic activity, accompanied by conformational changes and subunit rearrangements, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process
pyruvate
-
allosteric substrate activation, activation mechanism
pyruvate
-
allosteric substrate activation, alternating sites mechanism, random binding of pyruvate in the regulatory and active site, regulatory pyruvate is first bound to C-221 on the beta domain, binding generates a signal which is transmitted to the thiamine diphosphate cofactor, signal pathway, study of the pH-dependence of activation, two-step phenomenological model of activation, kinetics, pyruvate and pyruvamide have different activation pathways with distinct binding sites
pyruvate
-
allosteric substrate activation, kinetics of dimeric and tetrameric enzyme
pyruvate
-
hysteretic substrate activation, Cys-221 binds pyruvate to transmit the information to H-92, E-91, W-412, G-413 and finally to the active center thiamine diphosphate
pyruvate
-
substrate activation pathway from C221 to H92 to E91 to W412 to G413 to thiamine diphosphate, role of W412
pyruvate
-
substrate activation pathway, the consequences of binding substrate at C221 are propagated to the active site via the pathway H92 to E91 to W412 to G413 to thiamine diphosphate, role of C221 and E91
pyruvate
-
substrate activation, interaction of pyruvate with residue C221 provides the trigger, transmitting the information along the C221 to H92 to E91 to W412 to G413 pathway to the 4-amino nitrogen of the thiamine diphosphate cofactor, changes in hydrogen bonding at the active center as a result of substrate activation, mechanism
pyruvate
-
substrate activation, mechanism
pyruvate
allosteric substrate activation, binding of substrate at a regulatory site induces catalytic activity, accompanied by conformational changes and subunit rearrangements
pyruvate
substrate activator is allosterically bound to enzyme, mechanism
pyruvate
substrate activation
additional information
no substrate activation, PDC activity is regulated in response to growth substrate, highest with lactic acid, lower with ethanol or glycerol, and absent with mannitol
-
additional information
-
no substrate activation, PDC activity is regulated in response to growth substrate, highest with lactic acid, lower with ethanol or glycerol, and absent with mannitol
-
additional information
-
the membrane components in whole cells are sufficient for optimal (R)-phenylacetylcarbinol production and no further surfactant addition is required for optimal performance, in vitro cell debris or cell membrane components enhance the (R)-phenylacetylcarbinol production, overview
-
additional information
-
PDC activity in lowland and upland Cyperus rotundus tubers collected from several locations increases significantly when both ecotypes are subjected to hypoxia for 24 h following germination
-
additional information
-
enhanced PDC activity is observed in the skin tissue of fruit at early maturity stages
-
additional information
-
lack of substrate activation in Neurospora crassa yeast pyruvate decarboxylase species
-
additional information
induction of pdc1 is possibly a longterm response and pdc2 a short term response
-
additional information
-
induction of pdc1 is possibly a longterm response and pdc2 a short term response
-
additional information
-
growth on a medium with oxythiamine increases enzyme activity, but may be in response to an earlier inhibition of enzyme leading to an accumulation of pyruvate, which induces the biosynthesis of enzyme apoform
-
additional information
-
glucose induces the enzyme not through a single signalling pathway, but involving several pathways, glucose sensors Gpr1, Snf3 and Rgt2 are not required, mutational analysis, overview
-
additional information
PDC1 is expressed during aerobic growth on glucose and is upregulated 4fold in response to oxygen limitation, PDC1 expression is lower in cells grown on ethanol and succinate than on glucose and is up regulated 2-4fold, respectively, after glucose addition
-
additional information
-
PDC1 is expressed during aerobic growth on glucose and is upregulated 4fold in response to oxygen limitation, PDC1 expression is lower in cells grown on ethanol and succinate than on glucose and is up regulated 2-4fold, respectively, after glucose addition
-
additional information
-
not activated by the substrate pyruvate
-
additional information
-
high glycolytic and ethanologenic fluxes correlate with enhanced transcription and enzymatic activity levels of PDC
-
additional information
-
PDC activity in KO11 is limiting and hence positively controls the flux to ethanol formation, since a 7fold amplification of its activity causes a 1.3fold increase into the ethanol flux, increased PDC activity stimulates glucose and xylose consumption rates
-
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1.7 - 40
2-keto-4-methylhexanoic acid
4.7 - 50
2-ketobutanoic acid
2.86
2-Ketobutyrate
30°C, wild-type PDC
2.2
2-ketobutyric acid
-
in 100 mM MES buffer (pH 5.6), 5 mM MgCl2, 1 mM dithiothreitol, and 1 mM thiamine diphosphate, at 25°C
0.2 - 12.7
2-ketohexanoic acid
2.5 - 11
2-ketopentanoic acid
12.9
2-ketovalerate
30°C, wild-type PDC
2.42
2-oxoisocaproate
pH 7.0, 30°C
1.27
2-oxoisopentanoate
-
-
1.9 - 7.73
2-oxoisovalerate
12.9
2-oxomethylvalerate
pH 7.0, 30°C
additional information
additional information
-
1.7
2-keto-4-methylhexanoic acid
mutant I472A, pH 6.5, 30°C
3.7
2-keto-4-methylhexanoic acid
mutant I472A/I476F, pH 6.5, 30°C
40
2-keto-4-methylhexanoic acid
and above, wild type, pH 6.5, 30°C
4.7
2-ketobutanoic acid
wild type, pH 6.5, 30°C
6.7
2-ketobutanoic acid
mutant I472A, pH 6.5, 30°C
50
2-ketobutanoic acid
mutant I472A/I476F, pH 6.5, 30°C
0.2
2-ketohexanoic acid
mutant I472A, pH 6.5, 30°C
0.5
2-ketohexanoic acid
mutant I472A/I476F, pH 6.5, 30°C
12.7
2-ketohexanoic acid
wild type, pH 6.5, 30°C
2.5
2-ketopentanoic acid
mutant I472A, pH 6.5, 30°C
7.6
2-ketopentanoic acid
wild type, pH 6.5, 30°C
11
2-ketopentanoic acid
mutant I472A/I476F, pH 6.5, 30°C
1.9
2-oxoisovalerate
pH 6.5, 37°C
7.73
2-oxoisovalerate
pH 7.0, 30°C
1.8
benzoylformate
mutant I472A, pH 6.5, 30°C
4.4
benzoylformate
mutant I472A/I476F, pH 6.5, 30°C
0.02
pyruvate
-
mutant enzyme A287G, at pH 6.0 and 30°C
0.042
pyruvate
-
in 100 mM MES buffer (pH 5.6), 5 mM MgCl2, 1 mM dithiothreitol, and 1 mM thiamine diphosphate, at 25°C
0.06
pyruvate
pH 5.0, 25°C
0.06
pyruvate
at pH 5.0 and 25°C
0.1
pyruvate
-
mutant enzyme S311A, at pH 6.0 and 30°C
0.1 - 2
pyruvate
-
pH 5.0, 55°C, recombinant enzyme
0.15
pyruvate
-
mutant enzyme E473D, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.18 - 0.2
pyruvate
-
30°C, E473D mutant PDC
0.24
pyruvate
-
pH 6, 30°C
0.25
pyruvate
pH 8.4, 80°C
0.25
pyruvate
-
30°C, D27E mutant PDC
0.3
pyruvate
-
mutant enzyme H92F, at pH 6.0 and 30°C
0.31
pyruvate
-
wild type enzyme, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.4
pyruvate
-
mutant enzyme E473Q, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.4
pyruvate
-
mutant enzyme C221A/C222A, at pH 6.5 and 10°C
0.43 - 0.48
pyruvate
-
30°C, D27N mutant PDC
0.5
pyruvate
-
mutant enzyme E50D
0.5
pyruvate
-
wild type enzyme, at pH 6.0 and 30°C
0.52
pyruvate
-
wild type enzyme and mutant enzyme E449D
0.55
pyruvate
-
histidine buffer, enzyme from healthy tissue
0.6
pyruvate
at pH 6.0 and 25°C
0.62
pyruvate
-
pH 6.2, 25°C
0.66 - 0.68
pyruvate
-
30°C, wild-type PDC
0.68
pyruvate
30°C, wild-type PDC
0.71
pyruvate
-
mutant enzyme H114Q
0.72
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51A
0.74
pyruvate
-
pH 6.0, 55°C, native enzyme
0.8
pyruvate
isoform PDC I, pH 6.0, 30°C
0.85
pyruvate
-
histidine buffer, enzyme from diseased tissue
0.86
pyruvate
-
mutant enzyme W487L
0.9
pyruvate
isoform PDC II, pH 6.0, 30°C
0.92
pyruvate
pH 8.4, 80°C
0.95
pyruvate
-
mutant enzyme D440E and mutant enzyme N467D
0.97
pyruvate
-
mutant enzyme F496I
1.04 - 1.17
pyruvate
-
30°C, E473Q mutant PDC
1.06
pyruvate
-
mutant enzyme F496H
1.1
pyruvate
wild type, pH 6.5, 30°C
1.1
pyruvate
-
wild-type, pH 6.5, 30°C
1.1
pyruvate
-
pH and temperature not specified in the publication
1.1
pyruvate
-
per subunit, pH 6.0, 30°C, wild-type enzyme
1.1
pyruvate
-
mutant L112A, pH 6.5, 30°C
1.2
pyruvate
pH 7.0, 25°C
1.2
pyruvate
at pH 7.0 and 25°C
1.2
pyruvate
-
pH 6.5, 55°C, recombinant enzyme
1.25
pyruvate
-
pH 6.2, 25°C, presence of 0.1 M NaCl
1.33
pyruvate
-
mutant enzyme V111A
1.4
pyruvate
pH 8.4, 80°C
1.47
pyruvate
-
per subunit, pH 6.0, 30°C, mutant C221E/C222A
1.66
pyruvate
-
per subunit, pH 6.0, 30°C, mutant D28A
1.7
pyruvate
-
phosphate buffer, enzyme from healthy tissue
1.73
pyruvate
pH 6, 25°C, sigmoidal dependence of the reaction rate from substrate concentration, Hill coefficient 2.10
1.79
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E91D
2.3
pyruvate
-
phosphate buffer, enzyme from diseased tissue
2.3 - 6
pyruvate
-
pH 6.0, 37°C
2.5
pyruvate
-
in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
2.6
pyruvate
mutant I476F, pH 6.5, 30°C
2.8
pyruvate
pH 6.5, potassium MES buffer, two affinities for pyruvate, sigmoidal kinetics
2.8
pyruvate
-
in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
2.8
pyruvate
-
pH 7.0, 55°C, recombinant enzyme
3.02
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E477Q
3.4
pyruvate
-
mutant N482D, pH 6.5, 30°C
3.6
pyruvate
-
at pH 6.5 and 50°C
3.9
pyruvate
pH 6.5, 35C, isozyme 1
4.5
pyruvate
pH 6.5, 35°C, isozyme 2
4.7
pyruvate
-
mutant I476L, pH 6.5, 30°C
6.8
pyruvate
-
mutant I476A, pH 6.5, 30°C
7.8
pyruvate
mutant I472A, pH 6.5, 30°C
8.9
pyruvate
-
mutant I476V, pH 6.5, 30°C
9.1
pyruvate
-
mutant I472A, pH 6.5, 30°C
10
pyruvate
pH 6.5, sodium hydrogen maleate buffer, two affinities for pyruvate, sigmoidal kinetics
14.9
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51Q
16
pyruvate
-
mutant enzyme H310F, at pH 6.0 and 30°C
23.1
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51D
31.5
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51N
50
pyruvate
mutant I472A/I476F, pH 6.5, 30°C
18
Pyruvic acid
-
pH 6.0, 30°C, recombinant mutant V461I
22
Pyruvic acid
-
pH 6.0, 30°C, recombinant mutant M538W
34
Pyruvic acid
-
pH 6.0, 30°C, recombinant mutant S286Y
65
Pyruvic acid
-
pH 6.0, 30°C, recombinant mutant F381W
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic data, kinetic model
-
additional information
additional information
-
kinetic data, pH-dependence of steady-state kinetic parameters
-
additional information
additional information
-
kinetic data, pH-dependence of steady-state kinetic parameters of wild-type, W412F and W412A mutant PDC
-
additional information
additional information
-
kinetic model, kinetic data
-
additional information
additional information
-
kinetic model, Km values for different conformations of wild-type enzyme at different pH values between pH 4.5 and 6.5
-
additional information
additional information
-
kinetic parameters for carboligase reactions of wild-type and mutant YPDC
-
additional information
additional information
-
pH-dependent kinetic data of wild-type, C221E/C222A and C221A/C222A double mutant YPDC
-
additional information
additional information
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle
-
additional information
additional information
-
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle
-
additional information
additional information
-
kinetics analysis of the wild-type enzyme with beta-hydroxypyruvate as substrate in the decarboxylation reaction
-
additional information
additional information
-
pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetic parameters for beta-hydroxypyruvate
-
additional information
additional information
the isozyme shows sigmoidal kinetics with a Hill coefficient of 1.8
-
additional information
additional information
the isozyme shows sigmoidal kinetics with a Hill coefficient of 1.8
-
additional information
additional information
-
binding affinity of CoA is 0.11 mM
-
additional information
additional information
-
steady-state kinetic analysis, overview. The v/[S] plots display negative cooperativity and hence deviate from Michaelis-Menten kinetics in just the opposite way
-
additional information
additional information
-
the recombinant enzyme expressed in Geobacillus thermoglucosidasius shows normal Michaelis-Menten kinetics with pyruvate
-
additional information
additional information
-
transient state, pre-steady-state, and steady-state complex formations of substrate/intermediate and thiamine diphosphate cofactor and of kinetics of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.4 - 8.1
2-keto-4-methylhexanoic acid
9 - 320
2-ketobutanoic acid
0.8 - 130
2-ketohexanoic acid
11 - 220
2-ketopentanoic acid
13.7
2-ketovalerate
30°C, wild-type PDC
additional information
additional information
-
0.4
2-keto-4-methylhexanoic acid
wild type, pH 6.5, 30°C
7.7
2-keto-4-methylhexanoic acid
mutant I472A, pH 6.5, 30°C
8.1
2-keto-4-methylhexanoic acid
mutant I472A/I476F, pH 6.5, 30°C
9
2-ketobutanoic acid
mutant I472A/I476F, pH 6.5, 30°C
32
2-ketobutanoic acid
mutant I476F, pH 6.5, 30°C
250
2-ketobutanoic acid
mutant I472A, pH 6.5, 30°C
320
2-ketobutanoic acid
wild type, pH 6.5, 30°C
9
2-Ketobutyrate
30°C, wild-type PDC
61.4
2-Ketobutyrate
30°C, wild-type PDC
0.8
2-ketohexanoic acid
mutant I476F, pH 6.5, 30°C
4
2-ketohexanoic acid
wild type, pH 6.5, 30°C
82
2-ketohexanoic acid
mutant I472A/I476F, pH 6.5, 30°C
130
2-ketohexanoic acid
mutant I472A, pH 6.5, 30°C
11
2-ketopentanoic acid
mutant I476F, pH 6.5, 30°C
30
2-ketopentanoic acid
mutant I472A/I476F, pH 6.5, 30°C
53
2-ketopentanoic acid
wild type, pH 6.5, 30°C
220
2-ketopentanoic acid
mutant I472A, pH 6.5, 30°C
1.2
benzoylformate
mutant I472A/I476F, pH 6.5, 30°C
6.9
benzoylformate
mutant I472A, pH 6.5, 30°C
0.0024
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51N
0.0043
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51A
0.03 - 0.55
pyruvate
-
pH 6, 25°C, W412A mutant PDC
0.035
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51Q
0.049
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E51D
0.066
pyruvate
-
per subunit, pH 6.0, 30°C, mutant D28A
0.086
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E477Q
0.1
pyruvate
-
mutant enzyme E473D, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.15
pyruvate
-
mutant enzyme E473Q, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.99
pyruvate
-
pH 6, 25°C, C221E/C222A double mutant YPDC
2.1
pyruvate
-
pH 6, 25°C, wild-type PDC
2.5
pyruvate
-
pH 6, 4°C, C221A/C222A double mutant PDC
3.1
pyruvate
-
pH 6, 25°C, E91A mutant PDC
3.8
pyruvate
-
pH 6, 25°C, C221D/C222A double mutant YPDC
5 - 7
pyruvate
-
pH 5.0, 55°C, recombinant enzyme
6.1
pyruvate
-
kcat per monomer, pH 7.0, 25°C
6.55
pyruvate
-
pH 6, 25°C, W412A mutant PDC
8
pyruvate
mutant I472A/I476F, pH 6.5, 30°C
8.6
pyruvate
at pH 7.0 and 25°C
10
pyruvate
-
pH 6, 4°C, wild-type PDC
11
pyruvate
-
per subunit, pH 6.0, 30°C, mutant E91D
12.5
pyruvate
-
kcat per monomer, pH 6.5, 25°C
14
pyruvate
-
kcat per monomer, pH 6.0, MES-NaOH buffer, 25°C
15
pyruvate
-
pH 6, 30°C, C221A/C222A double mutant PDC
16.9
pyruvate
-
kcat per monomer, pH 5.5, 25°C
17.2
pyruvate
-
kcat per monomer, pH 5.0, 25°C
17.5
pyruvate
-
pH 6, 25°C, E91D mutant PDC
17.8
pyruvate
-
pH 6, 25°C, W412F mutant PDC
18.2
pyruvate
-
per subunit, pH 6.0, 30°C, mutant C221E/C222A
18.3
pyruvate
-
kcat per monomer, pH 6.0, phosphate buffer, 25°C
20.4
pyruvate
-
pH 6, 25°C, E91Q mutant PDC
40
pyruvate
-
pH 6, 30°C, enzyme monomer
43.6
pyruvate
isoform PDC I, pH 6.0, 30°C
47
pyruvate
-
pH 6.5, 55°C, recombinant enzyme
60
pyruvate
-
per subunit, pH 6.0, 30°C, wild-type enzyme
65
pyruvate
isoform PDC6, at pH 7.0 and 25°C
73.1
pyruvate
-
pH 6, 25°C, wild-type PDC
77
pyruvate
isoform PDC II, pH 6.0, 30°C
77
pyruvate
mutant I476F, pH 6.5, 30°C
113
pyruvate
30°C, wild-type PDC
113
pyruvate
-
at pH 7.0 and 50°C
125
pyruvate
-
pH 7.0, 55°C, recombinant enzyme
145
pyruvate
isoform PDC1, at pH 7.0 and 25°C
150
pyruvate
-
wild type enzyme, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
200
pyruvate
mutant I472A, pH 6.5, 30°C
207
pyruvate
isoform PDC5, at pH 7.0 and 25°C
486
pyruvate
wild type, pH 6.5, 30°C
580
pyruvate
-
at pH 6.5 and 50°C
2.3
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant V461I
2.5
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant M538W
17
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant S286Y
26
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant F381W
additional information
additional information
-
-
-
additional information
additional information
-
kcat values at different pH values from pH 4.5 to 7.5 of wild-type, W412F and W412A mutant PDC
-
additional information
additional information
-
kcat values of wild-type, C221E/C222A and C221A/C222A double mutant YPDC at different pH values between pH 5 and 7.2
-
additional information
additional information
-
kinetic model, kcat values for different conformations of wild-type enzyme at different pH values between pH 4.5 and 6.5
-
additional information
additional information
-
kinetic parameters for carboligase reactions of wild-type and mutant YPDC
-
additional information
additional information
values for several C-terminal deletion mutants
-
additional information
additional information
-
values for several C-terminal deletion mutants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.02 - 0.03
-
pH 6, 20°C, D28A mutant YPDC
0.04 - 0.07
-
pH 6, 20°C, D28N mutant YPDC
0.1
-
crude extract, at 25°C
0.1 - 0.15
-
pH 6, 20°C, E477Q mutant YPDC
0.15
substrate 2-oxo-4-methylpentanoate, pH 5.0, 25°C
0.29
-
30°C, growth on ethanol, aerobic conditions
0.4
-
using 4-methyl-2-oxohexanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.5
-
using 3-(1H-indol-3-yl)-2-oxopropanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.64
-
30°C, growth on galactose, aerobic conditions
0.68
substrate 2-oxopentanoate, pH 5.0, 25°C
0.8
-
using phenylpyruvate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.95
-
30°C, growth on glucose, aerobic conditions
1.45
wild-type, pH 7.0, 60°C
1.7
-
using 2-oxo-4-phenylbutanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
1.8
-
using phenylpyruvate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
1.81
-
30°C, growth on glucose, anaerobic conditions
10.4
-
using 3-methyl-2-oxobutanoate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
12
substrate 2-oxobutanoate, pH 5.0, 25°C
12.9
-
using 2-oxopentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
125
-
with pyruvate, pH 7.0, 55°C, recombinant enzyme
14.34
-
after 143fold purification, at 25°C
147
-
using pyruvate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
16.9
-
using 2-oxobutanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
18.8
-
using 2-oxopentanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
2.2
-
using 3-methyl-2-oxopentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
20
substrate pyruvate, pH 5.0, 25°C
20.7
-
using 2-oxopentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
21.24
-
substrate 2-oxoisocaproate, pH 6.0, 37°C
21.7
isoform PDC I, pH 6.0, 30°C
26.77
-
substrate 2-oxoisovalerate, pH 6.0, 37°C
3.71
-
diseased preparations
3.8
purified enzyme, pH 8.4, 80°C
4.2
-
using 2-oxohexanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
4.4
-
with pyruvate, pH 6.0, 55°C, native enzyme
4.51
mutant Y35N/K139R/V172A/H474R, pH 7.0, 60°C
40
isoform PDC II, pH 6.0, 30°C
40 - 45
-
pH 6, 20°C, wild-type YPDC
43
substrate pyruvate, pH 7.0, 25°C
43.4
-
using pyruvate as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
45 - 50
-
pH 6, 25°C, wild-type PDC
47
-
with pyruvate, pH 6.5, 55°C, recombinant enzyme
5.3
-
using 2-oxohexanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
5.52
mutant H747R, pH 7.0, 60°C
5.7
-
pH 6.2, 25°C, metronidazole-resistant strain
515
-
pH 6, 25°C, C221A/C222A double mutant PDC
57
-
with pyruvate, pH 5.0, 55°C, recombinant enzyme
59.4
purified native isozymes
6.2
-
using 2-oxohexanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
6.9
-
using 3-methyl-2-oxobutanoate as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
60
-
using 2-oxobutanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
75.4
purified native isozyme
85.1
-
using 2-oxobutanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
89.3
-
using pyruvate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.046
50°C, pH 6.0
0.2
-
using 2-oxo-5-phenylpentanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
0.2
-
using 2-oxo-5-phenylpentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
using 2-oxo-4-phenylbutanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
using 3-fluoro-2-oxopropanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
using 4-methyl-2-oxopentanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
using 2-oxo-4-phenylbutanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
using oxo(phenyl)acetic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.6
-
using 4-methyl-2-oxohexanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.6
-
using 2-oxooctanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.6
-
using 3-fluoro-2-oxopropanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
1.1
-
using 11 as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
1.1
-
using 2-oxooctanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
1.1
-
using 4-methyl-2-oxopentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
12.3
-
-
12.3
-
healthy preparations
2.8
-
using 3-methyl-2-oxopentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
2.8
-
using 4-methyl-2-oxopentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
additional information
-
additional information
-
-
additional information
-
(R)-phenylacetylcarbinol production rate
additional information
-
(R)-phenylacetylcarbinol production rate
additional information
-
-
additional information
-
-
additional information
-
(R)-phenylacetylcarbinol production rate
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
activity in cell extracts grown on different media estimated with and without exogenous thiamine diphosphate
additional information
-
carboligase reaction, wild-type and mutant YPDC, at different pH values
additional information
-
no difference in specific activity of dimeric and tetrameric enzyme state
additional information
-
(R)-phenylacetylcarbinol production rate
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
-
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
-
-
additional information
-
-
additional information
-
colorimetric assay based on formation of (R)-phenylacetylcarbinol
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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12000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
120000 - 128000
dimeric enzyme form, native PAGE
13000
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
14000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
22000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
220000 - 240000
-
gel filtration
23000
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
235000
recombinant PDC, pH 6.5, gel filtration
244000
active enzyme, gel filtration
26000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
272000
tetrameric enzyme form, native PAGE
39800
-
1 * 39800 + 1 * 41700, the dimeric pyruvate decarboxylase is a component of the multienzyme complex pyruvate dehydrogenase, SDS-PAGE
41700
-
1 * 39800 + 1 * 41700, the dimeric pyruvate decarboxylase is a component of the multienzyme complex pyruvate dehydrogenase, SDS-PAGE
45000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
56500
-
4 * 56500, SDS-PAGE
57000
-
4 * 57000, SDS-PAGE
58700
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
58873
x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
59400
2 * 59400, calculated from amino acid sequence
60746
-
4 * 60746, SDS-PAGE
61320
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
61468
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
61486
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
61500
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
61600
alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
61821
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
63000
-
x * 63000, SDS-PAGE
64000
x * 64000, alpha-subunit + x * 62000, beta-subunit
65300
x * 65300, calculated
200000
-
gel filtration
200000
-
about, gel filtration
200000
about, wild-type PDC, gel filtration
240000
-
240000
-
disc gel electrophoresis
240000
-
native tetrameric PDC
240000
-
wild-type and E473Q mutant PDC, gel filtration
35000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
35000
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
35000
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
46000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
46000
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
58000
4 * 58000, recombinant PDC, pH 6.5, SDS-PAGE
58000
-
x * 58000, recombinant enzyme, SDS-PAGE
59000
-
4 * 59000, SDS-PAGE
59000
-
x * 60800, about, sequence calculation, x * 59000, recombinant His-tagged enzyme, SDS-PAGEs
59200
-
59200
x * 59200, calculated, x * 60000, SDS-PAGE
60000
-
SDS-PAGE
60000
-
x * 60000, SDS-PAGE
60000
x * 60000, SDS-PAGE
60000
-
4 * 60000, SDS-PAGE
60000
-
4 * 60000, SDS-PAGE
60000
-
4 * 60000, SDS-PAGE
60000
-
4 * 60000, SDS-PAGE
60000
-
1 * 60000, alpha subunit, catalytically inactive form
60000
-
1 * 60000, catalytically inactive enzyme state, SDS-PAGE
60000
-
2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
60000
-
4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
60000
-
4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE
60000
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
60000
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
60000
x * 59200, calculated, x * 60000, SDS-PAGE
60800
-
-
60800
4 * 60800, wild-type PDC, SDS-PAGE
60800
-
x * 60800, about, sequence calculation, x * 59000, recombinant His-tagged enzyme, SDS-PAGEs
61000
alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
61000
4 * 61000, calculated, 4 * 66000, SDS-PAGE
61000
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
62000
-
4 * 62000, SDS-PAGE
62000
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
62000
x * 64000, alpha-subunit + x * 62000, beta-subunit
62000
-
x * 62000, recombinant enzyme, SDS-PAGE
66000
x * 66000, SDS-PAGE
66000
x * 66000, SDS-PAGE
66000
4 * 61000, calculated, 4 * 66000, SDS-PAGE
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dimer or tetramer
-
a tight dimer, known as the functional dimer, is the minimal catalytically active unit, two of these functional dimers assemble into a loose tetramer in the quaternary structure
heterotetramer
-
native, catalytically active form, dimer of dimers
homodimer
-
2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
oligomer
-
the enzyme forms filamentous structures at pH 6.0-6.5 of octamers and dodecamers, NcPDC tetramers display the lowest catalytic efficiency among all functional oligomeric forms of this enzyme, analysis by analytical gel filtration, analytical ultracentrifugation and small-angle X-ray solution scattering
?
x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
?
-
x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
-
?
-
x * 62590, calculated from amino acid sequence
?
x * 59200, calculated, x * 60000, SDS-PAGE
?
x * 59200, calaculated from amino acid sequence
?
-
x * 60000, SDS-PAGE
-
?
-
x * 59200, calaculated from amino acid sequence
-
?
-
x * 60800, about, sequence calculation, x * 59000, recombinant His-tagged enzyme, SDS-PAGEs
?
-
x * 60800, about, sequence calculation, x * 59000, recombinant His-tagged enzyme, SDS-PAGEs
-
?
-
x * 103400, maltose binding protein-bound isoform Pdc1p, calculated from amino acid sequence
?
-
x * 104900, maltose binding protein-bound isoform Pdc5p, calculated from amino acid sequence
?
-
x * 103400, maltose binding protein-bound isoform Pdc1p, calculated from amino acid sequence
-
?
-
x * 104900, maltose binding protein-bound isoform Pdc5p, calculated from amino acid sequence
-
?
x * 64000, alpha-subunit + x * 62000, beta-subunit
?
-
x * 60800, calculated from amino acid sequence
?
-
x * 60000, SDS-PAGE
-
?
-
x * 60800, calculated from amino acid sequence
-
?
-
2 protein bands detected in SDS-PAGE: 65000 and 68000, the enzyme exists as a mixture of tetramers, octamers and higher oligomers
?
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
?
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
?
-
x * 62000, recombinant enzyme, SDS-PAGE
?
-
x * 66000, SDS-PAGE
-
?
-
x * 58000, recombinant enzyme, SDS-PAGE
?
-
2 types of subunits, MW 61000 and MW 62000, SDS-PAGE
?
-
x * 60930, calculated from amino acid sequence
dimer
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
dimer
-
catalytically active form
dimer
-
1 * 39800 + 1 * 41700, the dimeric pyruvate decarboxylase is a component of the multienzyme complex pyruvate dehydrogenase, SDS-PAGE
dimer
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
dimer
-
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
-
homotetramer
-
-
homotetramer
-
4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
homotetramer
-
dimer of dimers, minimal catalytic unit is a functional dimer
homotetramer
-
dimer of dimers, minimal catalytic unit is a functional dimer, two active sites in the functional dimer act in an antiphase manner during the reaction, with each active site eventually completing the full catalytic cycle, study of subunit dissociation into two types of dimers depending on the experimental conditions and their reassociation
homotetramer
-
dimer of dimers, the minimal catalytic unit is the dimer with its active sites are not acting independently of one another, alternating sites model
homotetramer
4 * 58000, recombinant PDC, pH 6.5, SDS-PAGE
homotetramer
Sarcina ventriculi Goodsir / ATCC 55887
-
4 * 58000, recombinant PDC, pH 6.5, SDS-PAGE
-
homotetramer
alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
homotetramer
-
alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
-
homotetramer
2 * 59400, calculated from amino acid sequence
homotetramer
4 * 60800, wild-type PDC, SDS-PAGE
monomer
-
1 * 60000, alpha subunit, catalytically inactive form
monomer
-
1 * 60000, catalytically inactive enzyme state, SDS-PAGE
octamer
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
octamer
-
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
-
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
tetramer
subunit crystal structure analysis, the subunits are each composed of three domains, the R domain, the PYR domain, and the PP domain, all three domains exhibit typical alpha/beta-topology, the enzyme shows a half-side closed tetramer in presence or absence of any activator, the half-side closed form is predominant for Kluyveromyces lactis pyruvate decarboxylase, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process, overview
tetramer
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
-
tetramer
4 * 61000, calculated, 4 * 66000, SDS-PAGE
tetramer
-
4 * 62000-64000, SDS-PAGE
tetramer
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
tetramer
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
enzyme structure, differences in the tetramer assembly of form A and B PDC, form A is the native PDC
tetramer
subunit crystal structure analysis, the subunits are each composed of three domains, the R domain, the PYR domain, and the PP domain, all three domains exhibit typical alpha/beta-topology, the enzyme contains flexible loops comprising residues 106-113 and 292-301 involved in catalysis via four active sites, open and closed conformation of the activate and nonactivated enzyme, respectively, the completely open enzyme state is favoured for Saccharomyces cerevisiae pyruvate decarboxylase, overview
tetramer
-
enzyme structure, differences in the tetramer assembly of form A and B PDC, form A is the native PDC
-
tetramer
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
tetramer
-
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
-
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
4 * 56500, SDS-PAGE
tetramer
-
4 * 60746, SDS-PAGE
tetramer
-
two of the dimers form a tightly packed tetramer with pseudo 222 symmetry
tetramer
-
4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE
additional information
-
-
additional information
-
-
additional information
-
4 * 62000, SDS-PAGE
additional information
-
one isoenzyme has the subunit structure alpha4 and the other has the subunit structure alpha2'beta2
additional information
-
thiamine diphosphate is required for complete association of subunits to form active oligomer
additional information
-
different oligomeric states, tetramers, dimers and monomers, of enzyme occur under defined conditions, unfolding kinetics, tetramers dissociate via a stable dimeric state into monomers
additional information
-
treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
additional information
-
conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure
additional information
-
-
additional information
-
hydroxyl-ion-induced subunit dissociation
additional information
-
-
additional information
-
two types of protein chains detected by SDS-PAGE: MW 63000-65000 and MW 61000-62000
additional information
-
-
additional information
-
2 protein bands, MW 61000 and MW 60000, detected by SDS-PAGE of enzyme from kernels. 3 protein bands: MW 59000, 58000 and 44000, detected by SDS-PAGE of the enzyme from roots
additional information
-
phosphate stabilizes the tetramer by shifting the dimer-tetramer equilibrium to higher pH values, without altering the conformation of the tetramer
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D28A
-
the mutant is almost catalytically inactive
E477Q
-
the mutant is almost catalytically inactive
F381W
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme
M538W
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing higher kcat and activity with pyruvate compared to the wild-type enzyme
S286Y
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme
V461I
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing higher kcat and activity with pyruvate compared to the wild-type enzyme
A143T/T156A/Q367H/N396I/K478R
A287G
-
the mutant shows reduced activity compared to the wild type enzyme
C221D
-
mutant with nearly wild-type activity, hyperbolic kinetics
C221D/C222A
-
double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics
C221E
-
mutant with nearly wild-type activity, hyperbolic kinetics
C222A
-
still possesses 20-30% specific activity compared to the wild type enzyme and can still be inhibited by the (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid class of inhibitors/substrate analogues as well as cinnamaldehydes
D291A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
D291N
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced activity compared to the wild-type enzyme
E477Q/E91D
-
retains catalytic activity
E51A
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme,and the mutant is no longer capable of forming a hydrogen bond with cofactor thiamine diphosphate
E51D/E91D
-
no residual catalytic activity
E51N
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E51Q
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E91A
-
mutant with 30fold reduced specific activity, reduced turnover number and catalytic efficiency, abolished cooperativity, reduced thermal stability, impaired ability to bind the cofactors
E91Q
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency, abolished cooperativity, reduced thermal stability, impaired ability to bind the cofactors
H225F
-
the mutant shows reduced activity compared to the wild type enzyme
H310F
-
the mutant shows reduced activity compared to the wild type enzyme
H92F
-
the mutant shows wild type activity
L111A
-
site-directed mutagenesis, the mutant shows 47% of the wild-type kcat
L111Q
-
site-directed mutagenesis, the mutant shows 73% of the wild-type kcat
L111V
-
site-directed mutagenesis, the mutant shows 21% of the wild-type kcat
N293A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
S298A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
S300A
-
site-directed mutagenesis, the mutant shows altered kinetics with slightly reduced kcat compared to the wild-type enzyme
S311A
-
the mutant shows reduced activity compared to the wild type enzyme
T294A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
W412A
-
mutant with 10fold reduced specific activity, reduced turnover number and catalytic efficiency, very much reduced substrate activation, reduced affinity for thiamine diphosphate, reduced stability
W412F
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency
H747R
mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation
Y35N/K139R/V172A/H474R
shows 3.1fold higher acetaldehyde-forming activity than the wild-type
H747R
-
mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation
-
Y35N/K139R/V172A/H474R
-
shows 3.1fold higher acetaldehyde-forming activity than the wild-type
-
D27E
-
0.072% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
D27N
-
0.049% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
D440E
-
active, but unlike the wild type enzyme, exhibits a lag phase in product formation which can be reduced by preincubation with 5 mM thiamine diphosphate. Mutant N467D shows decreased affinity for thiamine diphosphate
E50D
-
2.9% of wild-type activity
E50Q
-
0.46% of wild-type activity
I472A
-
mutation influences the decarboxylation and carboligation reactions. The enlarged substrate-binding site allows the decarboxylation of longer aliphatic 2-keto acids (C4-C6) as well as aromatic 2-keto acids besides pyruvate, yielding hydroxypropiophenone, benzoin and phenylacetylcarbinol. Mutation impairs enantioselectivity
I472A/I476F
increase in substrate binding affinity and specificity, highest enantioselectivity for (S)-acetoin, very low yield of product
I476A
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476E
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476F
rapid loss of cofactor thiamine diphosphate. Improvement of enantioselectivity for (S)-acetoin
I476L
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476V
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
mutant I472A
2fold decrease in pyruvate decarboxylase activity, switch in substrate specificity to catalyse decarboxylation of benzoylformate, chimera between pyruvate decarboxylase and benzoylformate decarboxylase. Preferred substrates are 2-ketopentanoic acid and 2-ketohexanoic acid. Improvement of enantioselectivity for (S)-acetoin
N482D
-
mutation has a significant influence on the carboligation reaction, the binding of the cofactors and the thermostability are not affected
W329M
-
the carboligase activity of the mutant is 2.8% as high as the decarboxylase activity which is about 10fold higher than the wild type enzyme
W392M
-
higher carboligase/(R)-phenylacetylcarbinol-producing activity, more stable and higher resistance towards acetaldehyde than wild-type PDC
A143T/T156A/Q367H/N396I/K478R
-
mutant shows improved activity for 1 mM pyruvate at pH 7.5 in the presence of phosphate, has the substrate concentration required for half-saturation reduced by almost 3fold at pH 7.5 and the phosphate inhibition reduced by 4fold at pH 6.0 compared to the wild type enzyme, the mutant can be activated by pyruvate more easily than the native enzyme
A143T/T156A/Q367H/N396I/K478R
-
the mutant shows improved activity for 1 mM pyruvate at pH 7.5 in the presence of phosphate. In comparison with native Pdc1, the mutant has the substrate concentration required for half-saturation reduced by almost 3fold at pH 7.5 and the phosphate inhibition reduced by 4fold at pH 6.0, the apparent cooperativity for pyruvate is also reduced since it is activated by pyruvate more easily than the native enzyme
C221A
-
active mutant with reduced Hill coefficient of 1
C221A
-
mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6
C221A/C222A
-
active double mutant without substrate activation, effect of modified substrate-activation site on catalysis, kinetic properties
C221A/C222A
-
active double mutant, effect on transition states
C221A/C222A
-
the mutant shows reduced activity compared to the wild type enzyme
C221E/C222A
-
double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics
C221E/C222A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C221S
-
still possesses 20-30% specific activity compared to the wild type enzyme and can still be inhibited by the (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid class of inhibitors/substrate analogues as well as cinnamaldehydes
C221S
-
active mutant with reduced Hill coefficient of 0.8-0.9
C221S
-
mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6
C221S
-
mutant with abolished activation and reduced Hill coefficient
D28A
-
inactivated faster than the wild type enzyme
D28A
-
active site mutant with very low activity
D28A
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
D28A
-
lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction
D28A
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
D28A
the mutant is almost catalytically inactive
D28A
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
D28N
-
active site mutant with very low activity
D28N
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
D28N
-
lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction, higher acetoin formation than by wild-type YPDC
D28N
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
E477Q
-
inactivated faster than the wild type enzyme
E477Q
-
active site mutant with very low activity
E477Q
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
E477Q
-
active site mutant, kinetics, activation study of mutant enzyme
E477Q
-
lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction, higher acetoin formation than by wild-type YPDC
E477Q
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
E477Q
the mutant is almost catalytically inactive
E477Q
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
E51D
-
mutant with 50% of wild-type acetaldehyde producing activity
E51D
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E91D
-
mutant with 5fold reduced specific activity, reduced turnover number and catalytic efficiency, slightly reduced Hill coefficient, reduced thermal stability, impaired ability to bind the cofactors
E91D
-
racemic C2-alpha-lactylthiamine diphosphate exposed to mutant enzyme is partitioned between reversion to pyruvate and decarboxylation
E91D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H114F
-
inactivated faster than the wild type enzyme
H114F
-
active site mutant
H115F
-
inactivated faster than the wild type enzyme
H115F
-
active site mutant
E473D
-
inactive
E473D
-
0.173% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
E473D
-
the mutant exhibits a residual activity of 0.6% compared to the wild type enzyme, wild type PDC and the Glu473Asp variant bind the substrate analogue acetylphosphinate with the same affinity
E473Q
-
0.025% of wild-type specific activity, more tightly bound cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
E473Q
-
the mutant exhibits a residual activity of 0.1% compared to the wild type enzyme, Glu473Gln fails to bind the substrate analogue acetylphosphinate
additional information
generation of Gibberella zeae deletion strains containing a single deletion of each of the three PDC genes, and construction of a mutant strain with deletion of isozyme PDC1 and of acetyl-coenzyme A synthetase 1, ACS1. Deletion of the PDC1 gene results in suppression of ACS1-GFP expression
additional information
-
generation of Gibberella zeae deletion strains containing a single deletion of each of the three PDC genes, and construction of a mutant strain with deletion of isozyme PDC1 and of acetyl-coenzyme A synthetase 1, ACS1. Deletion of the PDC1 gene results in suppression of ACS1-GFP expression
additional information
-
each of isoform genes PDC11, PDC12, PDC13, can complement Saccharomyces cerevisiae pdc null mutant strains
additional information
production and phenotypic analysis of rice transgenics with altered levels of pyruvate decarboxylase protein, Pdc overexpressing rice transgenics at early seedling stage under unstressed control growth conditions showed slight, consistent advantage in root vigour as compared to that of wild-type seedlings, overview
additional information
-
production and phenotypic analysis of rice transgenics with altered levels of pyruvate decarboxylase protein, Pdc overexpressing rice transgenics at early seedling stage under unstressed control growth conditions showed slight, consistent advantage in root vigour as compared to that of wild-type seedlings, overview
additional information
-
enzyme null mutant, growth of mutant pollen tubes through the style is reduced, and the mutant allele shows reduced transmission through the male, when in competition with wild-type pollen
additional information
-
construction of mutant pdc-803 with a S296DELTAF297DELTA deletion, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
-
growth profile and ethanol production in isozyme knockout strains, overview
additional information
-
growth profile and ethanol production in isozyme knockout strains, overview
-
additional information
-
engineering of Lactobacillus brevis strain ATCC367 to express Sarcina ventriculi pyruvate decarboxylase and Lactobacillus brevis alcohol dehydrogenase genes in order to increase ethanol fermentation from biomass-derived residues, the engineered strain is termed bbc03, overview
additional information
engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data
additional information
-
engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data
additional information
-
enhancement of 1,3-propanediol production by expression of functional pyruvate decarboxylase and aldehyde dehydrogenase from Zymomonas mobilis in the acetolactate-synthase-deficient mutant of Klebsiella pneumoniae. The acetolactate synthase-deficient mutant of Klebsiella pneumoniae fails to produce 1,3-propanediol or 2,3-butanediol, and is defective in glycerol metabolism
additional information
-
enhancement of 1,3-propanediol production by expression of functional pyruvate decarboxylase and aldehyde dehydrogenase from Zymomonas mobilis in the acetolactate-synthase-deficient mutant of Klebsiella pneumoniae. The acetolactate synthase-deficient mutant of Klebsiella pneumoniae fails to produce 1,3-propanediol or 2,3-butanediol, and is defective in glycerol metabolism
-
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2 pyruvate decarboxylase genes diverge significantly from one another and from other yeast pyruvate decarboxylase genes
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expressed in Arabidopsis thaliana
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expressed in Clostridium thermocellum
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Rosetta 2 cells
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expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21(DE3)RecA- cells
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expressed in Escherichia coli JM109 cells
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expressed in Escherichia coli MC4100 cells
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expressed in Escherichia coli strain BL21
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expressed in Escherichia coli strain BL21(DE3)RecA-
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expressed in Escherichia coli strain KO11
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expressed in Escherichia coli strains CCE14 and KO11
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expressed in Escherichia coli TOP 10 cells
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expressed in Geobacillus thermoglucosidasius
expressed in Geobacillus thermoglucosidasius strain TN
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expressed in Hansenula polymorpha
expressed in Hansenula polymorpha strain NCYC495 leu1-1
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expressed in leaves of the Nicotiana tabacum transgenic line 9204-X
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expressed in pyruvate decarboxylase-deficient Saccharomyces cerevisiae strain D452-2
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expressed in the ethanol-tolerant Escherichia coli mutant ET1bc
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expression in Clostridium thermocellum
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
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expression in Saccharomyces cerevisiae, in a decarboxylase-negative pdc1Delta,pdc5Delta, pdc6Delta, aro10Delta background
expression of enzyme mutants in Escherichia coli strain BL21(DE3)
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expression of GFP-tagged isozyme PDC1 in both aerial and embedded mycelia, PDC1-GFP is highly expressed in both of types of mycelia
expression of mutants D28A and His6-tagged E477Q
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expression of pdc gene in recombinant Escherichia coli, sequencing, pdc operon
expression of PDC mutants D27E, D27N, E473D and E473Q in Escherichia coli
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expression of W412F and W412A mutant PDC in Escherichia coli BL21(DE3)
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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expression of wild-type and W392M mutant PDC in Escherichia coli K12
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expression of wild-type PDC and C-terminal deletion mutants in Escherichia coli
expression of wild-type, E91A, E91D and E91Q mutant PDC in Escherichia coli BL21(DE3)
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expression Ralstonia eutropha
fused with alcohol dehydrogenase and expressed in Escherichia coli JM109 cells
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gene pdc, co-expression with Lactobacillus brevis alcohol dehydrogenase in Lactobacillus brevis strain ATCC367 using a Gram-positive promoter, co-expression of both enzymes in Escherichia coli NZN111, a fermentative defective strain incapable of growing anaerobically, restores anaerobic growth and confers ethanol production
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gene pdc, recombinant expression in an acetolactate-synthase-deficient mutant of Klebsiella pneumoniae
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gene pdc, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, heterologous expression of the enzyme, passaged through Escherichia coli strain JM109 for DNA methylation, in the thermophile Geobacillus thermoglucosidasius strain TM89, using the the 170-bp promoter region of the lactate dehydrogenase gene Pldh from Geobacillus thermoglucosidasiusNCA1503, for ethanol production
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gene pdc1, DNA and amino acid sequence determination and analysis, cloning of the flanking regions, expression analysis, enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux, PDC1 is expressed during aerobic growth on glucose and is upregulated 4fold in response to oxygen limitation, PDC1 expression is lower in cells grown on ethanol and succinate than on glucose and is up regulated 2-4fold, respectively, after glucose addition
induction of pdc1 is possibly a longterm response and pdc2 a short term response, expression analysis of genes pdc1 and pdc2 in shoots of wild-type and recombinant seedlings, expression of mutant genes in calli of cultivar Pusa Basmati 1 via Agrobacterium tumefaciens strain EHA105 transformation
overexpression of wild-type and mutant YPDC in Escherichia coli BL21
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pdc gene, sequencing, expression in Escherichia coli BL-21-CodonPlus-RIL containing plasmid pSJS1240
PDC2 gene, overexpression improves the tolerance of hairy roots to low oxygen conditions
recombinant expression in Escherichia coli strain BL21(DE3)
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subcloning in Escherichia coli strain DH5alpha, expression in Escherichia coli strain BL21(DE3)plysS
subcloning in Escherichia coli strain DH5alpha, expression of C-terminally His-tagged isozymes in Escherichia coli strain BL21(DE3)plysS
wild type enzyme is expressed in Escherichia coli SG13009 cells, mutant enzymes E473D and E473Q are expressed in Escherichia coli JM109 cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Geobacillus thermoglucosidasius
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expressed in Geobacillus thermoglucosidasius
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expressed in Hansenula polymorpha
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expressed in Hansenula polymorpha
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expression in Escherichia coli
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expression in Escherichia coli
recombinant expression
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biotechnology
the reaction specificity of acetolactate synthase from Thermus thermophilus can be redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. Quadruple mutant Y35N/K139R/V172A/H474R shows 3.1fold higher acetaldehyde-forming activity than the wild-type mainly because of H474R amino acid substitution, which likely generates two new hydrogen bonds near the thiamine diphosphate-binding site
biotechnology
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the reaction specificity of acetolactate synthase from Thermus thermophilus can be redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. Quadruple mutant Y35N/K139R/V172A/H474R shows 3.1fold higher acetaldehyde-forming activity than the wild-type mainly because of H474R amino acid substitution, which likely generates two new hydrogen bonds near the thiamine diphosphate-binding site
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synthesis
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synthesis of (R)-phenylacetylcarbinol from cheap substrates in an aqueous reaction system by W392M mutant PDC, alternative strategy to the current fermentative process free of any unwanted by-product
synthesis
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Candida utilis PDC is a stable and high productivity enzyme for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
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engineered enzyme mutants are useful for synthesis of both enantiomers of alpha-ketols and acetolactates with good enantiomeric excess, overview
synthesis
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PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
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PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
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PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
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the enzyme is useful in ethanol production in bacterial coupled systems, overview
synthesis
alpha-ketoisovalerate decarboxylase Kivd from Lactococcus lactis combined with alcohol dehydrogenase Adh3 from Zymomonas mobilis are the optimum candidates for 3-methyl-1-butanol production in Corynebacterium glutamicum. The recombinant strain produces 0.182 g/l of 3-methyl-1-butanol and 0.144 g/l of isobutanol after 12 h of incubation. Further inactivation of the E1 subunit of pyruvate dehydrogenase complex gene (aceE) and lactic dehydrogenase gene (ldh) improves the 3-methyl-1-butanol titer to 0.497 g/l after 12 h of incubation
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
construction of a bypassed pyruvate decarboxylation pathway, through which pyruvate can be converted to acetyl-CoA, by using a coupled enzyme system consisting of pyruvate decarboxylase from Acetobacter pasteurianus and the CoA-acylating aldehyde dehydrogenase from Thermus thermophilus. A cofactor-balanced and CoA-recycling synthetic pathway for N-acetylglutamate production is designed by coupling the bypassed pathway with the glutamate dehydrogenase from Thermus thermophilus and N-acetylglutamate synthase from Thermotoga maritima. N-Acetylglutamate can be produced from an equimolar mixture of pyruvate and alpha-ketoglutarate with a molar yield of 55% through the synthetic pathway consisting of a mixture of four recombinant Escherichia coli strains having either one of the thermostable enzymes. The overall recycling number of CoA is 27
synthesis
construction of a bypassed pyruvate decarboxylation pathway, through which pyruvate can be converted to acetyl-CoA. The coupled enzyme system consists of pyruvate decarboxylase from Acetobacter pasteurianus and the CoA-acylating aldehyde dehydrogenase from Thermus thermophilus. A cofactor-balanced and CoA-recycling synthetic pathway for N-acetylglutamate production is established by coupling the bypassed pathway with the glutamate dehydrogenase from Thermus thermophilus and N-acetylglutamate synthase from Thermotoga maritima. N-Acetylglutamate can be produced from an equimolar mixture of pyruvate and alpha-ketoglutarate with a molar yield of 55% through the synthetic pathway consisting of a mixture of four recombinant Escherichia coli strains having either one of the thermostable enzymes. The overall recycling number of CoA is 27
synthesis
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construction of isobutanol production systems by overexpression of effective 2-oxoacid decarboxylase KivD and combinatorial overexpression of valine biosynthetic enzymes in Saccharomyces cerevisiae D452-2. Isobutanol production by the engineered strain is assessed in micro-aerobic batch fermentations using glucose as a sole carbon source, leading to priduction of 93 mg/l isobutanol, which corresponds to a fourfold improvement as compared with the control strain. Isobutanol production is further enhanced to 151 mg/l by additional overexpression of acetolactate synthase Ilv2p, acetohydroxyacid reductoisomerase Ilv5p, and dihydroxyacid dehydratase Ilv3p in the cytosol
synthesis
engineering of Klebsiella pneumoniae to produce 2-butanol from crude glycerol as a sole carbon source by expressing acetolactate synthase (IlvIH), keto-acid reducto-isomerase (IlvC) and dihydroxyacid dehydratase (IlvD) from Klebsiella pneumoniae, and alpha-oxoisovalerate decarboxylase (Kivd) and alcohol dehydrogenase (AdhA) from Lactococcus lactis. The engineered strain produce 2-butanol (160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol pathway by inactivating alpha-acetolactate decarboxylase (Adc) further improves the yield of 2-butanol from 160 to 320 mg/l
synthesis
enhancement of ethanol production capacity of Clostridium thermocellum by transferring pyruvate decarboxylase and alcohol dehydrogenase genes of the homoethanol pathway from Zymomonas mobilis. Both transferring pyruvate decarboxylase and alcohol dehydrogenase are functional in Clostridium thermocellum, but the presence of and alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene. The recombinant strain shows two-fold increase in pyruvate carboxylase activity and ethanol production when compared with the wild type strain
synthesis
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expression of branched-chain alpha-oxo acid decarboxylase from Lactococcus lactis subsp. lactis KivD and alcohol dehydrogenase from Zymomonas mobilis AdhB in Escherichia coli for higher alcohol production. In LB medium, the resulting strain produces much more 3-methyl-1-butanol (104 mg/l) than isobutanol (24 mg/l). In 5 g/l glucose-containing medium, the production of two alcohols is similar, 156 and 161 mg/l for C4 (isobutanol) and C5 (3-methyl-1-butanol) alcohol, respectively. The increase of glucose content and the adding of alpha-keto acids facilitate the production of C4 and C5 alcohols. The enzyme activities of pure Kivd on alpha-ketoisovalerate and alpha-ketoisocaproate are 26.77 and 21.24 micromol/min and mg, respectively
synthesis
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in order to increase production of isobutanol, 2-oxoacid decarboxylase (KDC) and alcohol dehydrogenase (ADH) are expressed in Saccharomyces cerevisiae to enhance the endogenous activity of the Ehrlich pathway. Overexpression Ilv2, which catalyzes the first step in the valine synthetic pathway, and deletion of the PDC1 gene encoding a major pyruvate decarboxylase alters the abundant ethanol flux via pyruvate. Along with modification of culture conditions, the isobutanol titer is elevated 13fold, from 11 mg/l to 143 mg/l, and the yield is 6.6 mg/g glucose
synthesis
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modification of enzyme with the N-succinimide ester of an amylose glycylglycine adduct. Upon conjugation, the optimum temperature shifts from 35°C to 40°C, the conjugate shows higher resistance to heat treatment than the native enzyme
synthesis
Ralstonia eutropha H16 produces polyhydroxybutanoate as an intracellular carbon storage material. The excess carbon can be redirected in engineered strains from polyhydroxybutanoate storage to the production of isobutanol and 3-methyl-1-butanol (branched-chain higher alcohols). Strains of Ralstonia eutropha with isobutyraldehyde dehydrogenase activity, in combination with the overexpression of plasmid-borne, native branched-chain amino acid biosynthesis pathway genes and the overexpression of heterologous ketoisovalerate decarboxylase gene, are employed for the biosynthesis of isobutanol and 3-methyl-1-butanol. One mutant strain produces over 180 mg/l branched-chain alcohols in flask culture, and is significantly more tolerant of isobutanol toxicity than wild-type. After the elimination of genes ilvE, bkdAB, and aceE, the production titer improves to 270 mg/l isobutanol and 40 mg/l 3-methyl-1-butanol. Under semicontinuous flask cultivation, the strain grows and produces more than 14 g/l branched-chain alcohols over the duration of 50 days
synthesis
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PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
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synthesis
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PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
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synthesis
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construction of isobutanol production systems by overexpression of effective 2-oxoacid decarboxylase KivD and combinatorial overexpression of valine biosynthetic enzymes in Saccharomyces cerevisiae D452-2. Isobutanol production by the engineered strain is assessed in micro-aerobic batch fermentations using glucose as a sole carbon source, leading to priduction of 93 mg/l isobutanol, which corresponds to a fourfold improvement as compared with the control strain. Isobutanol production is further enhanced to 151 mg/l by additional overexpression of acetolactate synthase Ilv2p, acetohydroxyacid reductoisomerase Ilv5p, and dihydroxyacid dehydratase Ilv3p in the cytosol
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synthesis
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expression of branched-chain alpha-oxo acid decarboxylase from Lactococcus lactis subsp. lactis KivD and alcohol dehydrogenase from Zymomonas mobilis AdhB in Escherichia coli for higher alcohol production. In LB medium, the resulting strain produces much more 3-methyl-1-butanol (104 mg/l) than isobutanol (24 mg/l). In 5 g/l glucose-containing medium, the production of two alcohols is similar, 156 and 161 mg/l for C4 (isobutanol) and C5 (3-methyl-1-butanol) alcohol, respectively. The increase of glucose content and the adding of alpha-keto acids facilitate the production of C4 and C5 alcohols. The enzyme activities of pure Kivd on alpha-ketoisovalerate and alpha-ketoisocaproate are 26.77 and 21.24 micromol/min and mg, respectively
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synthesis
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PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
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synthesis
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Candida utilis PDC is a stable and high productivity enzyme for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
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