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Information on EC 4.1.1.1 - pyruvate decarboxylase
for references in articles please use BRENDA:EC4.1.1.1
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IUBMB Comments
A thiamine-diphosphate protein. Also catalyses acyloin formation.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 4.1.1.1
- dendritic
-
plasmacytoid
-
toll-like
- thiamin
-
claim
- autoimmune
-
prescript
- ifn-alpha
-
pharmacy
-
lymphoid
-
herbicide
- zymomonas
-
branched-chain
- cdc
- acetaldehyde
- mobilis
- sulfonylurea
-
real-world
-
tregs
-
adhes
- interferon-alpha
-
insurance
-
lupus
-
antigen-presenting
- statin
-
costimulatory
-
lipoylated
- erythematosus
-
nonadherence
-
refill
-
medicare
-
tolerogenic
- dabigatran
- acetolactate
-
marketscan
-
dispensing
- synthesis
-
hla-dr
-
antimitochondrial
- acetoin
-
dihydrolipoyl
- biotechnology
-
pharmacist
-
herbicide-resistant
-
beneficiaries
-
icd-9-cm
- dihydrolipoamide
- transacetylase
- rivaroxaban
- dichloroacetate
-
enrollees
- lipoate
showSynonyms
pdc, pyruvate decarboxylase, acetohydroxyacid synthase, yeast pyruvate decarboxylase, pdc1p, p59nc, ifpl730, zmpdc, pyruvate decarboxylase 1, pdc5p, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2ODC
5TMA
8-10 nm cytoplasmic filament-associated protein
-
-
-
-
acetohydroxyacid synthase
-
the enzyme also has approximately 10% pyruvate decarboxylase activity
alpha-Carboxylase
-
-
-
-
alpha-Keto acid carboxylase
-
-
-
-
bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase
CgPDC
Decarboxylase, pyruvate
-
-
-
-
IpdC
KivD
KlPDC
P59NC
-
-
-
-
PDC
PDC I
PDC II
PDC1
Pdc1p
PDC2
PDC3
PDC4
Pdc5
Pdc5p
Pdc6
POR
-
bifunctional enzyme that catalyzes both the oxidative and nonoxidative decarboxylation of pyruvate
pyruvate decarboxylase 1
pyruvate decarboxylase 2
pyruvate decarboxylase 6
Pyruvic decarboxylase
-
-
-
-
scpdc1
ScPDC5
thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase
TTHA1213
YPDC
-
-
ZbPDC
ZmPDC
ZpPDC
additional information
bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase
-
bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase
-
-
PDC
-
-
-
-
PDC
-
-
Pdc6
-
sulfur-poor pyruvate decarboxylase, third minor isozyme of pyruvate decarboxylase
thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase
UniProt
thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase
UniProt
-
thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase
UniProt
-
additional information
see also EC 1.2.7.1, pyruvate-ferredoxin oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 2-oxo carboxylate = an aldehyde + CO2
catalytic mechanism, catalyzes the carboligation of 2 aldehydes as side reaction, mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
mechanism, catalyzes carboligation as side reaction
-
a 2-oxo carboxylate = an aldehyde + CO2
catalytic and kinetic mechanism, catalyzes carboligation as side reaction
-
a 2-oxo carboxylate = an aldehyde + CO2
-
-
-
-
a 2-oxo carboxylate = an aldehyde + CO2
catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions, thermodynamic data
-
a 2-oxo carboxylate = an aldehyde + CO2
catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions
-
a 2-oxo carboxylate = an aldehyde + CO2
Glu51 is the most important residue in formation of the ylide and the release of acetaldehyde. Glu477 and Asp28 are involved in decarboxylation of lactylthiamine diphosphate. Protonation of alpha-carbanion to form 2-(1-hydroxyethyl)-thiamine diphosphate goes through a concerted double proton transfer transition state involving both Asp28 and His115. Decarboxylation of lactylthiamine diphosphate and protonation of alpha-carbanion are two rate-limiting steps
-
a 2-oxo carboxylate = an aldehyde + CO2
in absence of substrate, equilibrium is shifted to 4'-aminopyridine thiamine diphosphate. Carbonyl group of substrate forms a hydrogen bond to Tyr290, geometry of substrate is well-suited for a nucleophilic attack by ylide-thiamine diphosphate
a 2-oxo carboxylate = an aldehyde + CO2
enzyme forms covalent intermediate C2-alpha-lactylthiamine diphosphate. Rate of reaction is limited by release of thiamine diphosphate
-
a 2-oxo carboxylate = an aldehyde + CO2
reaction mechanism, overview
-
a 2-oxo carboxylate = an aldehyde + CO2
mechanism of catalytic cycle of yeast pyruvate decarboxylase, overview. Pyruvate and analogues induce active site asymmetry in the wild-type yeast enzyme and mutant variants. The rare 1',4'-iminopyrimidine thiamine diphosphate tautomer participates in formation of thiamine diphosphate-bound intermediates. Propionylphosphinate also binds at the regulatory site and its binding is reflected by catalytic events at the active site 20 A away. The yeast enzyme stabilizes an electrostatic model for the 4'-aminopyrimidinium ionization state, an important contribution of the protein to catalysis
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboligation
decarboxylation
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
acetaldehyde biosynthesis II, butanol and isobutanol biosynthesis (engineered), L-methionine degradation III, long chain fatty acid ester synthesis (engineered), pyruvate fermentation to acetate VIII, pyruvate fermentation to acetoin III, pyruvate fermentation to ethanol II
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SYSTEMATIC NAME
IUBMB Comments
2-oxo-acid carboxy-lyase (aldehyde-forming)
A thiamine-diphosphate protein. Also catalyses acyloin formation.
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CAS REGISTRY NUMBER
COMMENTARY
9001-04-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-keto-4-methylhexanoic acid
3-methylpentanal + CO2
Substrates: -
Products: -
Products: -
?
2-ketobutyrate
?
Substrates: lower activity than with pyruvate
Products: -
Products: -
?
2-ketovalerate
?
Substrates: lower activity than with pyruvate
Products: -
Products: -
?
2-oxo-4-methylpentanoate
3-methylbutanaldehyde + CO2
Substrates: -
Products: -
Products: -
?
2-oxo-4-phenylbutanoic acid
3-phenylpropanal + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxo-5-phenylpentanoic acid
4-phenylbutanal + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxohexanoic acid
pentanal + CO2
-
Substrates: 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
Products: -
Products: -
?
2-oxomethylvalerate
?
Substrates: 16.7% of the activity with 2-oxoisovalerate
Products: -
Products: -
?
2-oxomethylvalerate
pentanal + CO2
Substrates: -
Products: -
Products: -
?
2-oxopentanoate
butanaldehyde + CO2
Substrates: -
Products: -
Products: -
?
2-oxopentanoic acid
butanal + CO2
-
Substrates: 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
Products: -
Products: -
?
3-(1H-indol-3-yl)-2-oxopropanoic acid
1H-indol-3-ylacetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
3-(1H-indol-3-yl)-2-oxopropanoic acid
?
-
Substrates: -
Products: -
Products: -
?
3-fluoro-2-oxopropanoic acid
fluoroacetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
-
Substrates: -
Products: -
Products: -
?
3-phenyl-2-oxopropanoate
?
Substrates: -
Products: -
Products: -
?
3-phenylpyruvate
2-phenylethanal + CO2
Substrates: 8.8% of the activity with 2-oxoisovalerate
Products: -
Products: -
?
4-methyl-2-oxohexanoic acid
3-methylpentanal + CO2
-
Substrates: -
Products: -
Products: -
?
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
-
Substrates: -
Products: -
Products: -
?
4-methylthio-2-oxobutanoate
3-methylthiopropanal + CO2
Substrates: 7.2% of the activity with 2-oxoisovalerate
Products: -
Products: -
?
acetaldehyde + benzaldehyde
(1R)-phenylacetylcarbinol
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + acetaldehyde
(R)-phenylacetylcarbinol
-
Substrates: -
Products: reaction proceeds under in vitro assay conditions, colorimetric assay based on reaction
Products: reaction proceeds under in vitro assay conditions, colorimetric assay based on reaction
?
benzaldehyde + pyruvate
(1R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
ir
benzaldehyde + pyruvate
L-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
?
benzoylformate
benzaldehyde + CO2
Substrates: substrate only for mutant mutant I472A
Products: -
Products: -
?
beta-hydroxypyruvate
2,4-dihydroxymethyl-3-oxo-butanoic acid
-
Substrates: D28A YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor
Products: -
Products: -
?
beta-hydroxypyruvate
glycolaldehyde + ?
-
Substrates: -
Products: -
Products: -
?
beta-hydroxypyruvate + glycolaldehyde
1,3,4-trihydroxy-2-butanone
-
Substrates: E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
Products: -
Products: -
?
indole-3-pyruvate
2-(indol-3-yl)-ethanal + CO2
Substrates: 0.1% of the activity with 2-oxoisovalerate
Products: -
Products: -
?
pyruvate + CoA + 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
Substrates: -
Products: -
Products: -
?
pyruvic acid
acetaldehyde + CO2
-
Substrates: 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
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
-
Substrates: D28A YPDC variant, not E477Q YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Zymomonas mobilis subsp. pomaceae Barker I
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Zymomonas mobilis subsp. pomaceae CCUG 17912
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Zymomonas mobilis subsp. pomaceae DSM 22645
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2-oxo-4-methylpentanoate
?
Substrates: -
Products: -
Products: -
?
2-oxo-4-methylpentanoate
?
Substrates: -
Products: -
Products: -
?
2-oxo-4-methylpentanoate
?
-
Substrates: -
Products: -
Products: -
?
2-Oxobutanoate
?
Substrates: -
Products: -
Products: -
?
2-Oxobutanoate
?
Substrates: -
Products: -
Products: -
?
2-oxobutanoate
propionaldehyde + CO2
Substrates: -
Products: -
Products: -
?
2-oxobutanoate
propionaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoisocaproate
3-methylbutanal + CO2
Substrates: 22.7% of the activity with 2-oxoisovalerate
Products: -
Products: -
?
2-oxoisocaproate
3-methylbutanal + CO2
Substrates: -
Products: -
Products: -
?
2-oxoisocaproate
3-methylbutanal + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoisocaproate
3-methylbutanal + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoisovalerate
2-methylpropanal + CO2
Substrates: -
Products: -
Products: -
?
2-oxoisovalerate
2-methylpropanal + CO2
Substrates: -
Products: -
Products: -
?
2-oxoisovalerate
2-methylpropanal + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoisovalerate
2-methylpropanal + CO2
-
Substrates: -
Products: -
Products: -
?
2-Oxopentanoate
?
Substrates: -
Products: -
Products: -
?
2-Oxopentanoate
?
Substrates: -
Products: -
Products: -
?
2-oxopentanoate
butyraldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
3-(indol-3-yl)pyruvate
2-(indol-3-yl)acetaldehyde + CO2
-
Substrates: activity of EC 4.1.1.74
Products: -
Products: -
?
3-(indol-3-yl)pyruvate
2-(indol-3-yl)acetaldehyde + CO2
-
Substrates: activity of EC 4.1.1.74
Products: -
Products: -
?
3-Fluoropyruvate
acetate + F- + CO2
-
Substrates: decarboxylation is followed by release of F-
Products: -
Products: -
?
3-Fluoropyruvate
acetate + F- + CO2
-
Substrates: decarboxylation is followed by release of F-
Products: -
Products: -
?
4-hydroxyphenylpyruvate
?
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + acetaldehyde
(S)-acetoin + ?
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + acetaldehyde
(S)-acetoin + ?
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + acetaldehyde
acetoin
-
Substrates: carboligation of 2 aldehydes as a side reaction of PDC
Products: -
Products: -
?
acetaldehyde + acetaldehyde
acetoin
-
Substrates: carboligation of 2 aldehydes as a side reaction of PDC
Products: -
Products: -
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
Substrates: carboligation of 2 aldehydes as a side reaction of PDC, high carboligase activity, more active than PDC from Zymomonas mobilis
Products: (R)-phenylacetylcarbinol
Products: (R)-phenylacetylcarbinol
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
Substrates: carboligation of 2 aldehydes as a side reaction of PDC, less active than PDC from Saccharomyces cerevisiae
Products: (R)-phenylacetylcarbinol
Products: (R)-phenylacetylcarbinol
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
-
Substrates: PDC can convert initial 100/120 mM benzaldehyde/pyruvate substrates to the statistical significantly highest maximum (R)-phenylacetylcarbinol (PAC) concentration (95.8 mM) and production rate (0.639 mM/min). PAC biotransformation profiles with initial benzaldehyde/pyruvate concentration of 100/120, 30/36, and 50/60 mM, mathematical modeling, PDC carboligase activity, overview
Products: -
Products: -
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
Candida tropicalis TISTR 5350
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
Candida tropicalis TISTR 5350
-
Substrates: PDC can convert initial 100/120 mM benzaldehyde/pyruvate substrates to the statistical significantly highest maximum (R)-phenylacetylcarbinol (PAC) concentration (95.8 mM) and production rate (0.639 mM/min). PAC biotransformation profiles with initial benzaldehyde/pyruvate concentration of 100/120, 30/36, and 50/60 mM, mathematical modeling, PDC carboligase activity, overview
Products: -
Products: -
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: transformation is enhanced by maintenance of neutral pH-value
Products: transformation is enhanced by maintenance of neutral pH-value
?
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
ir
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
ir
cinnamaldehyde
(2S,3R)-5-phenylpent-4-ene-2,3-diol + CO2
-
Substrates: -
Products: -
Products: -
?
cinnamaldehyde
(2S,3R)-5-phenylpent-4-ene-2,3-diol + CO2
-
Substrates: -
Products: -
Products: -
?
Phenylpyruvate
Phenylacetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
Phenylpyruvate
Phenylacetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
Substrates: enzyme catalyzes a carboligation as side reaction
Products: -
Products: -
?
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
Substrates: enzyme catalyzes a carboligation as side reaction
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: key enzyme for the oxidative metabolism of lactic acid
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Acetobacter pasteurianus NCIB 8618 / ATCC 12874
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Acetobacter pasteurianus NCIB 8618 / ATCC 12874
Substrates: key enzyme for the oxidative metabolism of lactic acid
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: ethanol fermentation pathway, involved in anaerobic metabolism
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: catalytic mechanism, contains catalytic and regulatory pyruvate binding site
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: catalytic cycle, overview
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: catalytic mechanism, contains catalytic and regulatory pyruvate binding site
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: Pdc is involved in the operation of ethanolic fermentation pathway that appears to correlate to an extent with anoxia tolerance in plants, overview
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: 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)
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: plus acetoin
Products: plus acetoin
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: plus acetoin
Products: plus acetoin
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: 3-4% acetoin side product
Products: 3-4% acetoin side product
?
pyruvate
acetaldehyde + CO2
-
Substrates: mechanism
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: catalytic mechanism
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: 4 active sites in the tetramer, enzyme structure
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: alternating sites mechanism
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: catalytic cycle, 3 domains: a diphosphate-binding domain, a pyrimidine-binding domain and a regulatory domain, model for enzyme regulation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: catalytic mechanism, acetaldehyde is produced by protonation of the key C2alpha-carbanion/enamine intermediate
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: detailed mechanism
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: 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
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: 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
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: nonoxidative decarboxylation, main reaction
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: 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
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: enzyme within the glycolytic pathway in fermenting cells
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: key role in the alcoholic fermentation process
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: penultimate step in the alcoholic fermentation process
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: penultimate step of alcohol fermentation
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: catalytic cycle, overview
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: 4 active sites in the tetramer, enzyme structure
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: penultimate step in the alcoholic fermentation process
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: only the undissociated pyruvic acid acts as the substrate
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: nonoxidative decarboxylation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
Substrates: nonoxidative decarboxylation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
Substrates: during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: in wild-type, about 10% of the acetolactate forming activity
Products: in wild-type, about 10% of the acetolactate forming activity
?
pyruvate
acetaldehyde + CO2
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: -
Products: in wild-type, about 10% of the acetolactate forming activity
Products: in wild-type, about 10% of the acetolactate forming activity
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: plus racemic acetoin
Products: plus racemic acetoin
?
pyruvate
acetaldehyde + CO2
Substrates: involved in the enhancement of ethanol production in berries, but not the limiting factor
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: first enzyme in a branch of glycolysis that converts pyruvate to ethanol
Products: first enzyme in a branch of glycolysis that converts pyruvate to ethanol
?
pyruvate
acetaldehyde + CO2
Substrates: key enzyme in alcoholic fermentation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: active site structure, catalytic mechanism
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: C-terminal region occludes the active site, enzyme structure, catalytic cycle, active site closure is required for decarboxylation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: 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
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: nonoxidative decarboxylation, main reaction
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: catalyzes the penultimate step in ethanol fermentation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
ethanal + CO2
Substrates: 0.6% of the activity with 2-oxoisovalerate
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
Products: i.e. 3-hydroxy-2-butanone, formation of the (R)- and the (S)-enantiomers
Products: i.e. 3-hydroxy-2-butanone, formation of the (R)- and the (S)-enantiomers
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: carboligation reaction
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: carboligation reaction
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: wild-type 100% conversion, 98% enantiomeric excess, mutant I472A, 60% conversion, 70% enantiomeric excess, mutant I476E, 6% conversion, 60% enantiomeric excess of S-enantiomer
Products: -
Products: -
?
pyruvate + phenylacetaldehyde
3-hydroxy-4-phenyl-butan-2-one + CO2
Substrates: enzyme catalyzes a carboligation as side reaction
Products: -
Products: -
?
pyruvate + phenylacetaldehyde
3-hydroxy-4-phenyl-butan-2-one + CO2
Substrates: enzyme catalyzes a carboligation as side reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: even with benzaldehyde as the only substrate no benzoin can be detected, the enzyme does not produce (S)-2-hydroxypropiophenone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the PAC biotransformation model for partially purified Candida tropicalis strain TISTR 5350 PDC consists of six rate equations that described the main product (PAC) formation, substrates (pyruvate and benzaldehyde) consumption, by-products (acetaldehyde and acetoin) formation, as well as deactivation of pyruvate decarboxylase with inorganic phosphate activation effect
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
Candida tropicalis TISTR 5350
-
Substrates: the PAC biotransformation model for partially purified Candida tropicalis strain TISTR 5350 PDC consists of six rate equations that described the main product (PAC) formation, substrates (pyruvate and benzaldehyde) consumption, by-products (acetaldehyde and acetoin) formation, as well as deactivation of pyruvate decarboxylase with inorganic phosphate activation effect
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in fruit ripening and aroma biogenesis
Products: -
Products: -
?
additional information
?
-
Substrates: involved in fruit ripening and aroma biogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
Products: -
Products: -
?
additional information
?
-
Substrates: involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 3-phenyl-2-oxopropanoate, benzoyl formate, and indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 3-phenyl-2-oxopropanoate, benzoyl formate, and indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activities of KivD, KP-IpdC, and variants of Kp-IpdC are determined by a coupled enzymatic method. The method is based on the ability of alcohol dehydrogenase, in the presence of NADH, to reduce aldehydes formed from 2-oxo acid by decarboxylase. The reaction is measured spectrophotometrically by the decrease in optical density at 340 nm. Pyruvate and 2-oxoisovalerate are used assubstrates individually
Products: -
Products: -
-
additional information
?
-
-
Substrates: enzyme activities of KivD, KP-IpdC, and variants of Kp-IpdC are determined by a coupled enzymatic method. The method is based on the ability of alcohol dehydrogenase, in the presence of NADH, to reduce aldehydes formed from 2-oxo acid by decarboxylase. The reaction is measured spectrophotometrically by the decrease in optical density at 340 nm. Pyruvate and 2-oxoisovalerate are used assubstrates individually
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform Pdc5p lacks enzymatic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform Pdc5p lacks enzymatic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of the engineered KdcA mutant enzymes with branched and unbranched 2-oxo acid substrates, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in ethanol formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in alcoholic fermentation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the penultimate step in alcohol fermentation
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in aerobic fermentation in mature pollen
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity is recorded on 3-phenyl-2-oxopropanoate, benzoylformate, 4-hydroxyphenylpyruvate, and indole-3-pyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes a carboligase reaction as side reaction forming acetoin and acetolactate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes also a carboligation as side reaction producing acetoin and acetolactate, mechanism, not: pyruvamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: pyruvamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: pyruvamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the role of the protein component of pyruvate decarboxylase in the mechanism of substrate activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not act on phenylpyruvate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the key enzymes involved in fermentation process
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in a pathway in which NAD+ is regenerated under anaerobic conditions
Products: -
Products: -
?
additional information
?
-
Substrates: nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
Products: -
Products: -
?
additional information
?
-
Substrates: nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: even with benzaldehyde as the only substrate no benzoin can be detected, the enzyme does not produce (S)-2-hydroxypropiophenone
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in ethanol formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in ethanol formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in glycolytic pathway to ethanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the penultimate step in alcohol fermentation
Products: -
Products: -
?
additional information
?
-
Substrates: PDC has no activity with benzoylformate
Products: -
Products: -
?
additional information
?
-
-
Substrates: PDC has no activity with benzoylformate
Products: -
Products: -
?
additional information
?
-
-
Substrates: pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
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?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Zymomonas mobilis subsp. pomaceae Barker I
Substrates: -
Products: -
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?
2 pyruvate
(S)-acetolactate + CO2
Zymomonas mobilis subsp. pomaceae CCUG 17912
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Zymomonas mobilis subsp. pomaceae DSM 22645
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
2 pyruvate
(S)-acetolactate + CO2
Substrates: -
Products: -
Products: -
?
3-(indol-3-yl)pyruvate
2-(indol-3-yl)acetaldehyde + CO2
-
Substrates: activity of EC 4.1.1.74
Products: -
Products: -
?
3-(indol-3-yl)pyruvate
2-(indol-3-yl)acetaldehyde + CO2
-
Substrates: activity of EC 4.1.1.74
Products: -
Products: -
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
Candida tropicalis TISTR 5350
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: key enzyme for the oxidative metabolism of lactic acid
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Acetobacter pasteurianus NCIB 8618 / ATCC 12874
Substrates: key enzyme for the oxidative metabolism of lactic acid
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: ethanol fermentation pathway, involved in anaerobic metabolism
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: Pdc is involved in the operation of ethanolic fermentation pathway that appears to correlate to an extent with anoxia tolerance in plants, overview
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: 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
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: enzyme within the glycolytic pathway in fermenting cells
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: key role in the alcoholic fermentation process
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: penultimate step in the alcoholic fermentation process
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: penultimate step of alcohol fermentation
Products: -
Products: -
ir
pyruvate
acetaldehyde + CO2
-
Substrates: regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: penultimate step in the alcoholic fermentation process
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
Substrates: during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
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?
pyruvate
acetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: involved in the enhancement of ethanol production in berries, but not the limiting factor
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
Substrates: key enzyme in alcoholic fermentation
Products: -
Products: -
?
pyruvate
acetaldehyde + CO2
-
Substrates: catalyzes the penultimate step in ethanol fermentation
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
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?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + acetaldehyde
acetoin + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: -
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
Substrates: stereospecific reaction, optimization of the biotransformation assay method
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in fruit ripening and aroma biogenesis
Products: -
Products: -
?
additional information
?
-
Substrates: involved in fruit ripening and aroma biogenesis
Products: -
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?
additional information
?
-
-
Substrates: involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
Products: -
Products: -
?
additional information
?
-
Substrates: involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in ethanol formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in alcoholic fermentation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the penultimate step in alcohol fermentation
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in aerobic fermentation in mature pollen
Products: -
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?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also performs carboligation reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: one of the key enzymes involved in fermentation process
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in a pathway in which NAD+ is regenerated under anaerobic conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in ethanol formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in ethanol formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in glycolytic pathway to ethanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the penultimate step in alcohol fermentation
Products: -
Products: -
?
additional information
?
-
-
Substrates: pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoA
-
desulfocoenzyme A can substitute for CoA showing that the cofactor plays a structural rather than a catalytic role
CoA
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
pyruvate ferredoxin oxidoreductase activity is strictly CoA-dependent, desulfo-CoA does not serve as cofactor. The pyruvate decarboxylase activity accepts desulfo-CoA, Km value for CoA is 0.0014 mM
CoA
the nonoxidative decarboxylation reaction catalyzed by PDC is dependent on CoA, Km is 420 nM
thiamine diphosphate
-
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
thiamine diphosphate
-
requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding
thiamine diphosphate
-
requirement, cofactor is located between the alpha and the gamma domains
thiamine diphosphate
-
requirement, active center, at the interface of the alpha and gamma domains
thiamine diphosphate
-
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
thiamine diphosphate
-
requirement, located at the active site at the interface of the alpha and gamma domains
thiamine diphosphate
-
coenzyme, bound in the interface between two subunits, binds pH-dependently
thiamine diphosphate
-
thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism
thiamine diphosphate
bound with high affinity at slightly acidic pH
thiamine diphosphate
-
enzyme forms covalent intermediate C2-alpha-lactylthiamine diphosphate
thiamine diphosphate
-
bound to the active site located at the interface of the alpha and gamma domains
thiamine diphosphate
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
thiamine diphosphate
dependent on, bound tightly, but not covalently, at the interface of two monomers
thiamine diphosphate
-
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
thiamine diphosphate
-
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
thiamine diphosphate
TPP, required for PDC activity, TPP is nonessential for pyruvate-ferredoxin oxidoreductase (POR) activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
0.5 mM, metal ions activate in descending order: Mg2+, Zn2+, Mn2+, Ca2+
Mg2+
Mn2+
-
0.5 mM, metal ions activate in descending order: Mg2+, Zn2+, Mn2+, Ca2+
Zn2+
-
0.5 mM, metal ions activate in descending order: Mg2+, Zn2+, Mn2+, Ca2+
Mg2+
-
0.5 mM, metal ions activate in the descending order: Mg2+, Zn2+, Mn2+, Ca2+
Mg2+
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of Mg2+ at pH above 8.0, leads to complete loss of activity
Mg2+
-
cofactor, tetramer binds 4 Mg2+ ions, tightly bound at pH 6, dissociates reversibly above pH 7
Mg2+
-
essential for activity, coordinated in the active site at the diphosphate moiety of the coenzyme thiamine diphosphate, also able to coordinate to other specific functional groups than in the active site region, stabilizes the monomeric state of enzyme
Mg2+
dependent on, bound tightly, but not covalently, at the interface of two monomers
Mg2+
-
cofactor, mode of active site binding, contains 1 mol Mg2+ per subunit
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
([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
-
-
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
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
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
-
wild type enzyme and mutant enzymes D28A, H114F, H115F and E477Q
acetaldehyde
-
inhibits, more resistant than PDC from Zymomonas mobilis, 8 mM, 2h, stable
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)
pyruvate
substrate inhibition at pyruvate concentrations above 20 mM for isoenzyme 1; substrate inhibition at pyruvate concentrations above 40 mM for isoenzyme 2
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
activation mechanism, binds only at the regulatory site, but with lower affinity than does pyruvate
Pyruvamide
-
activates, pyruvate and pyruvamide have different activation pathways with distinct binding sites
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
-
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
-
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
-
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
-
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
-
allosteric substrate activation, kinetics of dimeric and tetrameric enzyme
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 pathway from C221 to H92 to E91 to W412 to G413 to thiamine diphosphate, role of W412
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
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.98
3-(Indol-3-yl)pyruvate
-
recombinant mutant T290L, pH and temperature not specified in the publication
1.01
3-(Indol-3-yl)pyruvate
-
recombinant mutant L546W, pH and temperature not specified in the publication
1.48
3-(Indol-3-yl)pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
1.88
3-(Indol-3-yl)pyruvate
-
recombinant mutant Q383M, pH and temperature not specified in the publication
1.99
3-(Indol-3-yl)pyruvate
-
recombinant mutant V542I, pH and temperature not specified in the publication
2 - 3.4
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387I, pH and temperature not specified in the publication
5.91
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387L, pH and temperature not specified in the publication
15.85
3-(Indol-3-yl)pyruvate
-
recombinant mutant F388W, pH and temperature not specified in the publication
48.07
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387I/F388W, pH and temperature not specified in the publication
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
0.15
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
0.31
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
0.58
pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
1.3
pyruvate
pH and temperature not specified in the publication
1.73
pyruvate
pH 6, 25°C, sigmoidal dependence of the reaction rate from substrate concentration, Hill coefficient 2.10
1.9
pyruvate
pH and temperature not specified in the publication
2.5
pyruvate
-
in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
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
3.13
pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
9.1
pyruvate
pH and temperature not specified in the publication
10
pyruvate
pH 6.5, sodium hydrogen maleate buffer, two affinities for pyruvate, sigmoidal kinetics
11.6
pyruvate
pH and temperature not specified in the publication
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
-
kinetic parameters for carboligase reactions of wild-type and mutant YPDC
-
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
-
pH-dependent kinetic data of wild-type, C221E/C222A and C221A/C222A double mutant YPDC
-
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 data, kinetic model
-
additional information
additional information
-
pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview
-
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
-
kinetics analysis of the wild-type enzyme with beta-hydroxypyruvate as substrate in the decarboxylation reaction
-
additional information
additional information
-
steady-state kinetic parameters for beta-hydroxypyruvate
-
additional information
additional information
-
binding affinity of CoA is 0.11 mM
-
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
-
additional information
additional information
-
the recombinant enzyme expressed in Geobacillus thermoglucosidasius shows normal Michaelis-Menten kinetics with pyruvate
-
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
kinetic enzyme analysis, the PDC shows typical substrate cooperativity typical for yeast PDCs
-
additional information
additional information
kinetic enzyme analysis, the PDC shows typical substrate cooperativity typical for yeast PDCs
-
additional information
additional information
enzyme ApPDC demonstrates high kinetic stability
-
additional information
additional information
the enzyme follows Michaelis-Menten kinetics
-
additional information
additional information
the enzyme follows Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387L, pH and temperature not specified in the publication
0.704
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387I/F388W, pH and temperature not specified in the publication
1.51
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387I, pH and temperature not specified in the publication
2.59
3-(Indol-3-yl)pyruvate
-
recombinant mutant L546W, pH and temperature not specified in the publication
2.88
3-(Indol-3-yl)pyruvate
-
recombinant mutant V542I, pH and temperature not specified in the publication
2.9
3-(Indol-3-yl)pyruvate
-
recombinant mutant F388W, pH and temperature not specified in the publication
2.97
3-(Indol-3-yl)pyruvate
-
recombinant mutant T290L, pH and temperature not specified in the publication
4.18
3-(Indol-3-yl)pyruvate
-
recombinant mutant Q383M, pH and temperature not specified in the publication
8.05
3-(Indol-3-yl)pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
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
0.58
pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
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
additional information
additional information
values for several C-terminal deletion mutants
-
additional information
additional information
-
values for several C-terminal deletion mutants
-
additional information
additional information
-
kinetic parameters for carboligase reactions of wild-type and mutant YPDC
-
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
-
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
-
kcat values at different pH values from pH 4.5 to 7.5 of wild-type, W412F and W412A mutant PDC
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
3-(Indol-3-yl)pyruvate
-
recombinant mutant F388W, pH and temperature not specified in the publication
0.015
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387I/F388W, pH and temperature not specified in the publication
0.053
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387L, pH and temperature not specified in the publication
0.065
3-(Indol-3-yl)pyruvate
-
recombinant mutant A387I, pH and temperature not specified in the publication
0.173
3-(Indol-3-yl)pyruvate
-
recombinant mutant F388W, pH and temperature not specified in the publication
0.39
3-(Indol-3-yl)pyruvate
-
recombinant mutant L546W, pH and temperature not specified in the publication
0.691
3-(Indol-3-yl)pyruvate
-
recombinant mutant V542I, pH and temperature not specified in the publication
2.22
3-(Indol-3-yl)pyruvate
-
recombinant mutant Q383M, pH and temperature not specified in the publication
3.03
3-(Indol-3-yl)pyruvate
-
recombinant mutant T290L, pH and temperature not specified in the publication
5.44
3-(Indol-3-yl)pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.185
pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.38
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
0.58
pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.67
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
484
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000095
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphoryldifluoromethyl)phosphonic acid
-
-
0.0000012
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphorylmethyl) phosphonic acid
-
-
0.3
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethanol
-
-
0.00000003
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
0.00000002
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-5-methyl-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
0.00000003
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
-
0.00000002
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
-
0.4
mono(2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl) iminodiacetate
-
-
0.4
mono[2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl] malonate
-
-
0.00014
N-([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]sulfonyl)phosphoramidic acid
-
-
0.008
O-2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl sulfamate
-
-
0.00014
[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)sulfonyl]phosphoramidic acid
-
-
0.00000095
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl](difluoro)methyl]phosphonic acid
-
-
0.0000012
[[(2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethoxy)(hydroxy)phosphoryl]methyl]phosphonic acid
-
-
51
phosphate
-
mutant enzyme A143T/T156A/Q367H/N396I/K478R, at pH 6.0 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.046
0.15
substrate 2-oxo-4-methylpentanoate, pH 5.0, 25°C
0.2
0.3
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
0.6
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
1.1
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
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
12.3
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
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
2.8
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
3.8
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
43.4
-
using pyruvate as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
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
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
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
additional information
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 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 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 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 oxo(phenyl)acetic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
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
0.6
-
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 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
1.1
-
using 11 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
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
3.8
purified native enzyme, pH 9.5, 85°C
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
-
activity in cell extracts grown on different media estimated with and without exogenous thiamine diphosphate
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
-
colorimetric assay based on formation of (R)-phenylacetylcarbinol
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5
5.7 - 6.3
5.8
6 - 6.5
6.3
6.3 - 6.7
6.5
6.5 - 7
-
carboligation of acetaldehyde and benzaldehyde, optimal activity in potassium phosphate buffer
6.8
7.5
-
decarboxylation of hydroxypyruvate, negligible activity with pyruvate
8
-
synthesis of L-norephedrine in a coupled reaction with omega-transaminase from Vibrio fluvialis JS17
8.4
9.5
additional information
8.4
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity
8.4
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity
9.5
optimum in the absence of oxygen
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 8
-
pH 4.6: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
5.5 - 7
-
pH 5.5: about 60% of maximal activity, pH 7.0: about 45% of maximal activity
5.5 - 7.2
-
nearly identical Vmax values in the pH range, wild-type YPDC
6 - 11
activity range, profile overview. Inactive at pH 5.5
7
-
wild-type YPDC forms more acetaldehyde at higher pH, followed by a decrease above pH 7
8 - 11.5
-
pH 8.0: about 60% of maximal activity, pH 10.0: about 50% of maximal activity
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
40
-
enzyme modified with the N-succinimide ester of an amylose glycylglycine adduct
45
53
55
65
85
90
95
above 95°C, activity is highly temperature dependent
30
-
the optimal temperature for Pdc1 activity is dependent upon pyruvate concentration, in 1 mM pyruvate, native Pdc1 performs optimally at 30°C
30
-
synthesis of L-norephedrine in a coupled reaction with omega-transaminase from Vibrio fluvialis JS17
45
-
the optimal temperature for Pdc1 activity is dependent upon pyruvate concentration, in 25 mM pyruvate, native activity peaks at 45?C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
-
only slightly differing catalytic activity in the range, +/-10% relative to 25°C
30 - 102
activity range, profile overview
75 - 95
75°C: about 80% of maximal activity, 95°C: about 65% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Candida tropicalis TISTR 5306
nonpathogenic Candida tropicalis strain TISTR 5306 is isolated from Thai traditional rice wine
-
-
brenda
i.e. Komagataella pastoris, has a single isozyme
UniProt
brenda
isoforms Pdc11, Pdc12, Pdc13, overall enzyme activity is enhanced by glucose and oxygen limitation
-
-
brenda
no activity in Vibrio vulnificus
enzyme FrsAis not a cofactor-independent pyruvate decarboxylase. No pyruvate decarboxylase activity is detected for recombinant crystallized FrsA protein. The barrier to C-C bond cleavage in the bound substrate is 28 kcal/mol, which is similar to that estimated for the uncatalyzed decarboxylation of pyruvate in water at 25°C
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V9NGI4, i.e. subunit PorB, V9NFX1, i.e. subunit PorD, V9NGQ2 i.e. subunit PorG, V9NHA1 i.e. subunit PorA, bifunctional pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
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W8CQR1: subunit alpha, W8CQB2: subunit beta, W8CQB1: subunit gamma, W8CR61: subunit delta
UniProt
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W8CQR1: subunit alpha, W8CQB2: subunit beta, W8CQB1: subunit gamma, W8CR61: subunit delta
UniProt
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subunits alpha, beta, gamma and delta encoded by genes TK1983, TK1984, porG/TK1978, and TK1982
UniProt
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subunits alpha, beta, gamma and delta encoded by genes TK1983, TK1984, porG/TK1978, and TK1982
UniProt
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subunits alpha, beta, gamma and delta encoded by genes TK1983, TK1984, porG/TK1978, and TK1982
UniProt
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Q56317, i.e. subunit PorB, O05650, i.e. subunit PorC, Q56316 i.e. subunit PorD, O05651 i.e. subunit PorA, bifunctional pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase
-
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activity in metronidazole- or iron-restricted cells is 20-30 times higher than in metronidazole-sensitive strain
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-
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i.e. Candida pelliculosa or Hansenula anomala, diploid type strain NRRL-Y-366, haploid strain NRRL-Y-366-8, gene pdc1
SwissProt
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pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
-
-
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isozyme PDC1; four genes encoding PDC isozymes
UniProt
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nonpathogenic Candida tropicalis strain TISTR 5306 is isolated from Thai traditional rice wine
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gene product Fapdc1, induced during fruit ripening
Swissprot
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gene product Fapdc3, constitutively expressed in all tissues studied
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A0A068LJJ5 i.e. isoform PDC1, A0A068LJY3 i.e. isoform PDC2, A0A068LJB0 i.e. isoform PDC3
UniProt
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strain IFO005, isoforms PDC I and PDC II
Swissprot
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cultivar Pusa Basmati 1, genes pdc1 and pdc2, pdc gene family
Uniprot
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isozyme 1, gene pdcA; isozyme 1 encoded by gene pdcA
SwissProt
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isozyme 2, gene pdcB; isozyme 2 encoded by gene pdcB
SwissProt
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114284, 114286, 114291, 114293, 114294, 114299, 114300, 649851, 649910, 650049, 650079, 650080, 650144, 650152, 650161, 650541, 650671, 651089, 651094, 651741, 657568, 665596, 666155, 678162, 678579, 679923, 679924, 690937, 691578, 693587
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haploid strain expressing only one of three structural genes for pyruvate decarboxylase, PDC1
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isozyme PDC1; pyruvate decarboxylase isozyme 1
SwissProt
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isozyme PDC5; pyruvate decarboxylase isozyme 2, PDC5
UniProt
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isozyme PDC6; pyruvate decarboxylase isozyme 3, PDC6
UniProt
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isozyme PDC1; pyruvate decarboxylase isozyme 1
SwissProt
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isozyme PDC5; pyruvate decarboxylase isozyme 2, PDC5
UniProt
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isozyme PDC6; pyruvate decarboxylase isozyme 3, PDC6
UniProt
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Q56317, i.e. subunit PorB, O05650, i.e. subunit PorC, Q56316 i.e. subunit PorD, O05651 i.e. subunit PorA, bifunctional pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase
-
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expression in Haloferax volcanii, growth-phase dependent decrease in amount of enzyme protein
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wild type and mutant enzymes E50D, E50Q, V111A, H113Q, H114Q, D440N, D440T, D440G, D440E, E449D, N467Q, N467D, W487L, F496I, F496H
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
PDC2 appears to be leaf-specific
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isoform PDC2 is predominantly present in leaves
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PDC1 is expressed both in the aerial and embedded mycelia
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PDC1 is predominantly present in roots
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isoform PDC1 is predominantly present in roots
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PDC protein level is quite high in roots, even under aerobic conditions
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PDC protein level is quite high in roots, even under aerobic conditions
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additional information
PDC expression is high under aerobic conditions. High level of PDC protein observed by immunoblotting in aerobic tissues
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additional information
PDC expression is high under aerobic conditions. High level of PDC protein observed by immunoblotting in aerobic tissues
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additional information
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PDC expression is high under aerobic conditions. High level of PDC protein observed by immunoblotting in aerobic tissues
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additional information
growth profile and ethanol production in isozyme knockout strains, overview
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additional information
growth profile and ethanol production in isozyme knockout strains, overview
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additional information
growth profile and ethanol production in isozyme knockout strains, overview
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additional information
-
growth profile and ethanol production in isozyme knockout strains, overview
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additional information
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growth profile and ethanol production in isozyme knockout strains, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Sarcina ventriculi Goodsir / ATCC 55887
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recombinant PDC, expressed in Escherichia coli
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Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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the enzyme is a member of the superfamily of thiamine diphosphate-dependent enzymes
evolution
yet all available Thermococcals genome sequence do not have PDC or acetyl dehydrogenase (AcDH) gene homologues, thus Thermococcals as well as hyperthermophilic archaeaseem to use POR with additional PDC activity for dual function
evolution
-
yet all available Thermococcals genome sequence do not have PDC or acetyl dehydrogenase (AcDH) gene homologues, thus Thermococcals as well as hyperthermophilic archaeaseem to use POR with additional PDC activity for dual function
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evolution
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yet all available Thermococcals genome sequence do not have PDC or acetyl dehydrogenase (AcDH) gene homologues, thus Thermococcals as well as hyperthermophilic archaeaseem to use POR with additional PDC activity for dual function
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malfunction
mutations in both PDC1 and PDC2 result in lower tolerance to submergence
malfunction
deletion of PDC1 results in highly wettable mycelia, deletion of the PDC1 gene results in suppression of GFP-tagged acetyl-coenzyme A synthetase 1 expression
malfunction
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deletion of the Ser/Thr protein phosphatase SIT4 phosphatase decreases the pyruvate decarboxylase activity
malfunction
Saccharomyces cerevisiae TATA-box-binding protein SPT15 mutant spt15_Ala101Thr shows enhanced isoprenoid pathway flux. Metabolic flux analysis of the spt15_Ala101Thr mutant initially reveals a rerouting of the central carbon metabolism for the production of the precursor acetyl-CoA through activation of pyruvate-acetaldehyde-acetate cycle in the cytoplasm due to high flux in the reaction caused by pyruvate decarboxylase (PDC). This leads to alternate routes of cytosolic NADPH generation, and increased mitochondrial ATP production and phosphate demand in the mutant strain. Comparison of the transcriptomics of the spt15_Ala101Thr mutant cell with SPT15 wild-type cells shows upregulation of phosphate mobilization genes and pyruvate decarboxylase 6 (PDC6). Increasing the extracellular phosphate leads to an increase in the growth rate and biomass but diverts flux away from the isoprenoid pathway. PDC6 is also shown to play a critical role in isoprenoid pathway flux under phosphate limitation conditions. Transcriptome profile analysis of the mutant strain indicating upregulation of phosphate pathway and pyruvate decarboxylase, detailed overview
malfunction
the growth penalty associated with the lack of functional ADH1 or both PDC1 and PDC2 is greater under aerobic conditions than in hypoxia, highlighting the importance of fermentative metabolism in plants grown under normal, aerobic conditions. Effect of waterlogging and submerging on the phenotype of Arabidopsis thaliana wild-type and pdc1/pdc2 mutant plants, detailed overview
malfunction
-
mutations in both PDC1 and PDC2 result in lower tolerance to submergence
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malfunction
-
the growth penalty associated with the lack of functional ADH1 or both PDC1 and PDC2 is greater under aerobic conditions than in hypoxia, highlighting the importance of fermentative metabolism in plants grown under normal, aerobic conditions. Effect of waterlogging and submerging on the phenotype of Arabidopsis thaliana wild-type and pdc1/pdc2 mutant plants, detailed overview
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malfunction
-
deletion of the Ser/Thr protein phosphatase SIT4 phosphatase decreases the pyruvate decarboxylase activity
-
malfunction
-
Saccharomyces cerevisiae TATA-box-binding protein SPT15 mutant spt15_Ala101Thr shows enhanced isoprenoid pathway flux. Metabolic flux analysis of the spt15_Ala101Thr mutant initially reveals a rerouting of the central carbon metabolism for the production of the precursor acetyl-CoA through activation of pyruvate-acetaldehyde-acetate cycle in the cytoplasm due to high flux in the reaction caused by pyruvate decarboxylase (PDC). This leads to alternate routes of cytosolic NADPH generation, and increased mitochondrial ATP production and phosphate demand in the mutant strain. Comparison of the transcriptomics of the spt15_Ala101Thr mutant cell with SPT15 wild-type cells shows upregulation of phosphate mobilization genes and pyruvate decarboxylase 6 (PDC6). Increasing the extracellular phosphate leads to an increase in the growth rate and biomass but diverts flux away from the isoprenoid pathway. PDC6 is also shown to play a critical role in isoprenoid pathway flux under phosphate limitation conditions. Transcriptome profile analysis of the mutant strain indicating upregulation of phosphate pathway and pyruvate decarboxylase, detailed overview
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malfunction
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Saccharomyces cerevisiae TATA-box-binding protein SPT15 mutant spt15_Ala101Thr shows enhanced isoprenoid pathway flux. Metabolic flux analysis of the spt15_Ala101Thr mutant initially reveals a rerouting of the central carbon metabolism for the production of the precursor acetyl-CoA through activation of pyruvate-acetaldehyde-acetate cycle in the cytoplasm due to high flux in the reaction caused by pyruvate decarboxylase (PDC). This leads to alternate routes of cytosolic NADPH generation, and increased mitochondrial ATP production and phosphate demand in the mutant strain. Comparison of the transcriptomics of the spt15_Ala101Thr mutant cell with SPT15 wild-type cells shows upregulation of phosphate mobilization genes and pyruvate decarboxylase 6 (PDC6). Increasing the extracellular phosphate leads to an increase in the growth rate and biomass but diverts flux away from the isoprenoid pathway. PDC6 is also shown to play a critical role in isoprenoid pathway flux under phosphate limitation conditions. Transcriptome profile analysis of the mutant strain indicating upregulation of phosphate pathway and pyruvate decarboxylase, detailed overview
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metabolism
activities of pyruvate decarboxylase and alcohol dehydrogenase are required for the fermentative pathway, with ethanol as the predominant end product. Not only isozyme PDC1 but also isozyme PDC2 play a role under hypoxic conditions. The enzyme has a role under aerobic conditions, which is not coupled to fermentative metabolism
metabolism
activities of pyruvate decarboxylase and alcohol dehydrogenase are required for the fermentative pathway, with ethanol as the predominant end product
metabolism
-
pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeast Saccharomyces cerevisiae, mechanism of regulation of pyruvate decarboxylase activity, overview
metabolism
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
metabolism
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
metabolism
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
metabolism
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
metabolism
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
metabolism
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metabolic pathway of isobutanol synthesis and branch pathway in Klebsiella pneumoniae, overview. Kp-IpdC is catalyses the pyruvate decarboxylase activity as well as the 2-oxoisovalerate decarboxylation and further conversion to isobutanol. It is suspected that the pyruvate decarboxylase activity of Kp-IpdC reduces the available pyruvate for isobutanol synthesis
metabolism
role of phosphate limitation and pyruvate decarboxylase in rewiring of the metabolic network for increasing flux towards isoprenoid pathway in a TATA binding protein mutant of Saccharomyces cerevisiae. PDC6 plays a critical role in isoprenoid pathway flux under phosphate limitation conditions, detailed overview
metabolism
the enzyme is involved in the acetaldehyde production pathway, overview
metabolism
-
activities of pyruvate decarboxylase and alcohol dehydrogenase are required for the fermentative pathway, with ethanol as the predominant end product. Not only isozyme PDC1 but also isozyme PDC2 play a role under hypoxic conditions. The enzyme has a role under aerobic conditions, which is not coupled to fermentative metabolism
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metabolism
-
activities of pyruvate decarboxylase and alcohol dehydrogenase are required for the fermentative pathway, with ethanol as the predominant end product
-
metabolism
-
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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metabolism
-
pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeast Saccharomyces cerevisiae, mechanism of regulation of pyruvate decarboxylase activity, overview
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metabolism
-
role of phosphate limitation and pyruvate decarboxylase in rewiring of the metabolic network for increasing flux towards isoprenoid pathway in a TATA binding protein mutant of Saccharomyces cerevisiae. PDC6 plays a critical role in isoprenoid pathway flux under phosphate limitation conditions, detailed overview
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metabolism
-
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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metabolism
-
the enzyme is involved in the acetaldehyde production pathway, overview
-
metabolism
-
role of phosphate limitation and pyruvate decarboxylase in rewiring of the metabolic network for increasing flux towards isoprenoid pathway in a TATA binding protein mutant of Saccharomyces cerevisiae. PDC6 plays a critical role in isoprenoid pathway flux under phosphate limitation conditions, detailed overview
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metabolism
Nakaseomyces glabratus ATCC 2001
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pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
-
metabolism
-
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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metabolism
-
the enzyme is involved in the acetaldehyde production pathway, overview
-
metabolism
-
metabolic pathway of isobutanol synthesis and branch pathway in Klebsiella pneumoniae, overview. Kp-IpdC is catalyses the pyruvate decarboxylase activity as well as the 2-oxoisovalerate decarboxylation and further conversion to isobutanol. It is suspected that the pyruvate decarboxylase activity of Kp-IpdC reduces the available pyruvate for isobutanol synthesis
-
metabolism
-
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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metabolism
-
the enzyme is involved in the acetaldehyde production pathway, overview
-
metabolism
Nakaseomyces glabratus JCM 3761
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pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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metabolism
Nakaseomyces glabratus NBRC 0622
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pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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metabolism
Nakaseomyces glabratus NRRL Y-65
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pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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metabolism
-
pathway to produce ethanol and 1-butanol from lignocellulosic biomass via pyruvate decarboxylase (PDC): there are two major pathways for producing 1-butanol via pyruvate following the reaction of PDC, the CoA-dependent or the proline-dependent condensation, overview
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physiological function
isozymes PDC1 and PDC2 are involved in low-oxygen responses, whereas isozymes PDC3 and PDC4 are not affected by hypoxia/anoxia conditions
physiological function
roles of the three isozymes at different phases of Saccharomyces cerevisiae fermentation and with relevance for ethanol and carboligation reactions, overview
physiological function
PDC1 is required for lipid accumulation in the aerial mycelia. Isozyme PDC1 is also involved in vegetative growth of embedded mycelia in Gibberella zeae, possibly through initiating the ethanol fermentation pathway
physiological function
-
the enzyme is essential for directing the glucose flux to ethanol production. The activity of Pdc1p is regulated by phosphorylation of serine residues during growth
physiological function
pyruvate decarboxylase genes are involved in self-protection and defense in response to various abiotic and biotic stresses during rubber tree growth and development
physiological function
alpha-ketoisovalerate decarboxylase (kivD), BCAA-specific aminotransferase (bcaT) and C-S lyase (yjtE) gene expressions increase markedly by both isoleucine and valine starvation. Lactococcus lactis IFPL730 growth rate decreases under leucine, valine or isoleucine starvation but the strain reaches similar viable counts at the stationary phase in all culture conditions studied
physiological function
elimination of pyruvate decarboxylase activity in a pdc1 pdc5 pdc6 triple mutant virtually abolishes isobutyl alcohol production. Any single isozyme of pyruvate decarboxylase is sufficient for the formation of isobutyl alcohol from valine
physiological function
both isoforms PDC1 and PDC2 contribute to anoxia tolerance in Arabidopsis
physiological function
-
enzyme overexpression enhances ethanol production in Ogataea polymorpha
physiological function
-
the enzyme plays an important role in waterlogging resistance and heat stresses in kiwifruit
physiological function
-
pyruvate decarboxylase (PDC) is the crucial penultimate tetrameric enzyme in the ethanol formation process with the role of cleaving a carbon dioxide molecule from pyruvate through a decarboxylation catalytic step resulting in an active acetaldehyde. The proton consuming step of carbo-ligation reaction between active acetaldehyde and added PDC deactivating substrate-benzaldehyde on the active sites of PDC would result in the formation of precursor R-phenylacetylcarbinol (PAC) for production of well-known diastereomeric commercial bronchial dilators such as ephedrine and pseudoephedrine
physiological function
the enzyme is an extremely thermostable bifunctional enzyme, which exhibits pyruvate-ferredoxin oxidoreductase (POR, EC 1.2.7.1) and pyruvate decarboxylase (PDC) activities. The bifunctional enzyme is mainly involved in the catalysis of oxidative decarboxylation reaction of pyruvate (POR activity) to produce acetyl CoA but under certain conditions it also has the limited ability (PDC activity) to catalyze the nonoxidative decarboxylation of pyruvate to generate acetaldehyde
physiological function
-
the ipdC gene, annotated as an indole-3-pyruvate decarboxylase (Kp-IpdC, EC 4.1.1.74), is identified to catalyze the formation of isobutyraldehyde from 2-oxoisovalerate. Kp-IpdC exhibits promiscuous pyruvate decarboxylase activity, which adversely consume the available pyruvate precursor for isobutanol synthesis, computational modeling and mutational analysis. Kp-IpdC is more efficient than 2-oxoisovalerate decarboxylase from Lactococcus lactis (KivD) for 2-oxoisovalerate decarboxylation. Pyruvate decarboxylase activity is a limitation of Kp-IpdC
physiological function
enzyme PDC can act as an alternate route of metabolic manipulation for increasing the isoprenoid flux in yeast
physiological function
importance of alcohol dehydrogenase (ADH) and pyruvate decarboxylase (PDC) for aerobic plant growth. The two enzymes are key to the establishment of the fermentative metabolism in plants during oxygen shortage
physiological function
pyruvate decarboxylase (PDC) is responsible for the decarboxylation of pyruvate, producing acetaldehyde and carbon dioxide
physiological function
-
isozymes PDC1 and PDC2 are involved in low-oxygen responses, whereas isozymes PDC3 and PDC4 are not affected by hypoxia/anoxia conditions
-
physiological function
-
importance of alcohol dehydrogenase (ADH) and pyruvate decarboxylase (PDC) for aerobic plant growth. The two enzymes are key to the establishment of the fermentative metabolism in plants during oxygen shortage
-
physiological function
-
roles of the three isozymes at different phases of Saccharomyces cerevisiae fermentation and with relevance for ethanol and carboligation reactions, overview
-
physiological function
-
the enzyme is essential for directing the glucose flux to ethanol production. The activity of Pdc1p is regulated by phosphorylation of serine residues during growth
-
physiological function
-
enzyme PDC can act as an alternate route of metabolic manipulation for increasing the isoprenoid flux in yeast
-
physiological function
-
enzyme PDC can act as an alternate route of metabolic manipulation for increasing the isoprenoid flux in yeast
-
physiological function
-
the enzyme is an extremely thermostable bifunctional enzyme, which exhibits pyruvate-ferredoxin oxidoreductase (POR, EC 1.2.7.1) and pyruvate decarboxylase (PDC) activities. The bifunctional enzyme is mainly involved in the catalysis of oxidative decarboxylation reaction of pyruvate (POR activity) to produce acetyl CoA but under certain conditions it also has the limited ability (PDC activity) to catalyze the nonoxidative decarboxylation of pyruvate to generate acetaldehyde
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physiological function
-
the ipdC gene, annotated as an indole-3-pyruvate decarboxylase (Kp-IpdC, EC 4.1.1.74), is identified to catalyze the formation of isobutyraldehyde from 2-oxoisovalerate. Kp-IpdC exhibits promiscuous pyruvate decarboxylase activity, which adversely consume the available pyruvate precursor for isobutanol synthesis, computational modeling and mutational analysis. Kp-IpdC is more efficient than 2-oxoisovalerate decarboxylase from Lactococcus lactis (KivD) for 2-oxoisovalerate decarboxylation. Pyruvate decarboxylase activity is a limitation of Kp-IpdC
-
physiological function
-
alpha-ketoisovalerate decarboxylase (kivD), BCAA-specific aminotransferase (bcaT) and C-S lyase (yjtE) gene expressions increase markedly by both isoleucine and valine starvation. Lactococcus lactis IFPL730 growth rate decreases under leucine, valine or isoleucine starvation but the strain reaches similar viable counts at the stationary phase in all culture conditions studied
-
physiological function
-
enzyme overexpression enhances ethanol production in Ogataea polymorpha
-
physiological function
-
the enzyme is an extremely thermostable bifunctional enzyme, which exhibits pyruvate-ferredoxin oxidoreductase (POR, EC 1.2.7.1) and pyruvate decarboxylase (PDC) activities. The bifunctional enzyme is mainly involved in the catalysis of oxidative decarboxylation reaction of pyruvate (POR activity) to produce acetyl CoA but under certain conditions it also has the limited ability (PDC activity) to catalyze the nonoxidative decarboxylation of pyruvate to generate acetaldehyde
-
physiological function
-
pyruvate decarboxylase (PDC) is responsible for the decarboxylation of pyruvate, producing acetaldehyde and carbon dioxide
-
physiological function
Candida tropicalis TISTR 5306
-
pyruvate decarboxylase (PDC) is the crucial penultimate tetrameric enzyme in the ethanol formation process with the role of cleaving a carbon dioxide molecule from pyruvate through a decarboxylation catalytic step resulting in an active acetaldehyde. The proton consuming step of carbo-ligation reaction between active acetaldehyde and added PDC deactivating substrate-benzaldehyde on the active sites of PDC would result in the formation of precursor R-phenylacetylcarbinol (PAC) for production of well-known diastereomeric commercial bronchial dilators such as ephedrine and pseudoephedrine
-
additional information
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
additional information
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
additional information
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
additional information
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
additional information
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
additional information
-
homology three-dimensional structrue modeling of enzyme Kp-IpdC, 10 homologues with about 30% sequence identity to Kp-IpdC are selected as templates (PDB IDs 1OVM, 2VBF, 1QPB, 2W93, 2VK8, 2VJY, 1PVD, 1PYD, 2VK1, and 5NPU)
additional information
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
Nakaseomyces glabratus ATCC 2001
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
-
homology three-dimensional structrue modeling of enzyme Kp-IpdC, 10 homologues with about 30% sequence identity to Kp-IpdC are selected as templates (PDB IDs 1OVM, 2VBF, 1QPB, 2W93, 2VK8, 2VJY, 1PVD, 1PYD, 2VK1, and 5NPU)
-
additional information
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
Nakaseomyces glabratus JCM 3761
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
Nakaseomyces glabratus NBRC 0622
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
Nakaseomyces glabratus NRRL Y-65
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
additional information
-
besides acting as an important enzyme for ethanol production, PDC has also been applied in the in vitro production of n-butanol. Butanol together with other longer chain alcohols, such as 1-propanol, isobutanol and isopentanol, is regarded as the next-generation biofuel, due to its closer resemblance to traditional gasoline
-
Show AA Sequence and Transmembrane Helices (5234 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
13000
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
14000
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
200000
22000
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
23000
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
240000
26000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
35000
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
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
46000
58000
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
59000
59200
60000
60800
61000
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
62000
66000
35000
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
35000
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
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
59000
-
x * 60800, about, sequence calculation, x * 59000, recombinant His-tagged enzyme, SDS-PAGEs
59200
x * 59200, calculated, x * 60000, 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
-
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
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
62000
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
heterooctamer
homodimer
-
2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
homotetramer
monomer
octamer
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
tetramer
additional information
?
x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
?
Acetobacter pasteurianus NCIB 8618 / ATCC 12874
-
x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
-
?
x * 59200, calculated, 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
-
?
-
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
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
-
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
-
1 * 39800 + 1 * 41700, the dimeric pyruvate decarboxylase is a component of the multienzyme complex pyruvate dehydrogenase, SDS-PAGE
heterooctamer
dimer of heterotetramers (alphabetagammadelta)2, 1 * 44000, alpha-subunit, + 1 * 36000, beta-subunit + 1 * 20000, gamma-subunit, + 1 * 12000, delta-subunit, SDS-PAGE
heterooctamer
-
dimer of heterotetramers (alphabetagammadelta)2, 1 * 44000, alpha-subunit, + 1 * 36000, beta-subunit + 1 * 20000, gamma-subunit, + 1 * 12000, delta-subunit, SDS-PAGE
-
heterooctamer
-
dimer of heterotetramers (alphabetagammadelta)2, 1 * 44000, alpha-subunit, + 1 * 36000, beta-subunit + 1 * 20000, gamma-subunit, + 1 * 12000, delta-subunit, SDS-PAGE
-
homotetramer
-
the predicted Kp-IpdC structure is a homotetramer. Two monomers interact tightly to form the dimer, and two dimers form a tetramer. Each monomer consists of three domains with an open alpha/beta class topology: the N-terminal Pyr domain (residues 3-180), which binds the pyrimidine part of ThDP, the middle domain (residues 181-340), and the C-terminal PP domain (residues 356-551), which binds the diphosphate moiety of the cofactor per subunit. The Pyr and PP domains contain a six-stranded parallel beta-sheet flanked by a number of helices, whereas the middle domain contains a six-stranded mixed beta-sheet, with several helices packing against the sheet
homotetramer
-
the predicted Kp-IpdC structure is a homotetramer. Two monomers interact tightly to form the dimer, and two dimers form a tetramer. Each monomer consists of three domains with an open alpha/beta class topology: the N-terminal Pyr domain (residues 3-180), which binds the pyrimidine part of ThDP, the middle domain (residues 181-340), and the C-terminal PP domain (residues 356-551), which binds the diphosphate moiety of the cofactor per subunit. The Pyr and PP domains contain a six-stranded parallel beta-sheet flanked by a number of helices, whereas the middle domain contains a six-stranded mixed beta-sheet, with several helices packing against the sheet
-
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
-
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
-
4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, 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
-
octamer
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
octamer
-
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, 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
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
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
-
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
-
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
-
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
-
treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
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
-
conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure
additional information
-
two types of protein chains detected by SDS-PAGE: MW 63000-65000 and MW 61000-62000
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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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
Pdc1p is subject to reversible phosphorylation at Ser223 that is dependent on glucose availability, dephosphorylation of Pdc1p by alkaline phosphatase inhibits the enzyme activity by 50%. Phosphorylation of Pdc1p is dependent on the growth phase, being hyperphosphorylated in the logarithmic phase, dependent on the presence of Ser/Thr protein phosphatase SIT4p. The Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
phosphoprotein
-
Pdc1p is subject to reversible phosphorylation at Ser223 that is dependent on glucose availability, dephosphorylation of Pdc1p by alkaline phosphatase inhibits the enzyme activity by 50%. Phosphorylation of Pdc1p is dependent on the growth phase, being hyperphosphorylated in the logarithmic phase, dependent on the presence of Ser/Thr protein phosphatase SIT4p. The Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.69 A resolution, monoclinic space group C2 with cell dimensions: a = 129.1 A, b =141.0 A, c = 91.1 A, beta = 125.8°, with two monomers per asymmetric unit
hanging drop vapor diffusion method, using 20 mM citrate buffer, pH 6.1, 1 mM dithiothreitol, 5 mM thiamine diphosphate, 5 mM MgSO4, 20% (w/v) PEG 2000/PEG 6000 (1:1 ratio)
-
purified recombinant enzyme, 2 mg/ml protein in 50 mM MES, pH 6.45, 5 mM thiamine diphosphate, 1 mM dithiothreitol, and 5 mM MgSO4, or 35 mM sodium citrate, pH 6.45, 1 mM dithiothreitol, 5 mM thiamine diphosphate, and 5 mM MgSO4, in absence of ammonium sulfate, hanging drop vapour diffusion method, 8°C, in a 1:1 mixture with reservoir solution containing 20% w/v PEG 2000/PEG 8000 in crystallization buffer, microcrystals within 3 days, larger crystals within 4 weeks, X-ray diffraction structure determination and analysis at 2.26 A resolution
overexpression and downregulation of pdcI in transgenic Oryza sativa plants, pattern of expression, the alpha-subunit is encoded by pdc2 and that beta-subunit is encoded by pdc1
hanging drop vapor diffusion method, using 18 mM citrate/2 mM MES, pH 6.3, 2 mM dithiothreitol, 2 mM thiamine diphosphate, 2 mM MgSO4, 22.5% (w/v) PEG 2000/PEG 6000 (1:1 ratio)
hanging drop vapor diffusion method, using 0.15 M sodium citrate pH 5.5, 14% (w/v) PEG 3350
hanging drop vapor diffusion method, using 100 mM MES buffer (pH 6.0), 1 mM thiamin diphosphate, 5 mM MgSO4, and 20-24% (w/v) polyethylene glycol 1500
-
hanging drop vapor diffusion method, using potassium fluoride (0.2 M) and PEG 3350 (20% w/v), cocrystallization of PDC with pyruvate is conducted using a reservoir solution containing potassium chloride (0.2 M), PEG 3350 (17% w/v), and xylitol (3 or 1.5%, (w/v))
hanging drop vapor diffusion method, using 0.15 M sodium citrate pH 5.5, 14% (w/v) PEG 3350
-
hanging drop vapor diffusion method, using 0.15 M sodium citrate pH 5.5, 14% (w/v) PEG 3350
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A387I/F388W
-
site-directed mutagenesis, the mutant shows increased Km values for for pyruvate and for 2-oxoisovalerate are higher than those of the wild-type Kp-IpdC
A387L
D289L
-
site-directed mutagenesis, inactive mutant, the variant lost all decarboxylation activity with 2-oxoisovalerate and pyruvate
D289L/T290L
-
site-directed mutagenesis, inactive mutant, the variant lost all decarboxylation activity with 2-oxoisovalerate and pyruvate
F388W
-
site-directed mutagenesis, the mutant lost all activity to catalyze pyruvate decarboxylation and shows lower decarboxylation activity with 2-oxoisovalerate compared to wild-type
L546W
-
site-directed mutagenesis, the mutant shows 5.1% catalytic efficiency on pyruvate compared to wild-type Kp-IpdC
Q383M
-
site-directed mutagenesis, the mutant shows increased Km values for for pyruvate and for 2-oxoisovalerate are higher than those of the wild-type Kp-IpdC
T290L
-
site-directed mutagenesis, the mutant shows 22.1% catalytic efficiency on pyruvate compared to wild-type Kp-IpdC. Isobutanol production by Klebsiella pneumoniae T290L mutant is 25% higher than that of the control strain, and a final titer of 5.5 g/l isobutanol is obtained with a substrate conversion ratio of 0.16 mol/mol glucose. The T290L variant exhibits a decreased pyruvate decarboxylase activity
V542I
-
site-directed mutagenesis, the mutant shows increased Km values for for pyruvate and for 2-oxoisovalerate are higher than those of the wild-type Kp-IpdC
D289L
-
site-directed mutagenesis, inactive mutant, the variant lost all decarboxylation activity with 2-oxoisovalerate and pyruvate
-
D289L/T290L
-
site-directed mutagenesis, inactive mutant, the variant lost all decarboxylation activity with 2-oxoisovalerate and pyruvate
-
F388W
-
site-directed mutagenesis, the mutant lost all activity to catalyze pyruvate decarboxylation and shows lower decarboxylation activity with 2-oxoisovalerate compared to wild-type
-
L546W
-
site-directed mutagenesis, the mutant shows 5.1% catalytic efficiency on pyruvate compared to wild-type Kp-IpdC
-
T290L
-
site-directed mutagenesis, the mutant shows 22.1% catalytic efficiency on pyruvate compared to wild-type Kp-IpdC. Isobutanol production by Klebsiella pneumoniae T290L mutant is 25% higher than that of the control strain, and a final titer of 5.5 g/l isobutanol is obtained with a substrate conversion ratio of 0.16 mol/mol glucose. The T290L variant exhibits a decreased pyruvate decarboxylase activity
-
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
A101T
the transcriptome profile analysis of the mutant strain indicates the upregulation of phosphate pathway and pyruvate decarboxylase
A143T/T156A/Q367H/N396I/K478R
A287G
-
the mutant shows reduced activity compared to the wild type enzyme
C221A
C221A/C222A
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/C222A
C221S
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
D28A
D28N
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
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
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
E91D
E91Q
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency, abolished cooperativity, reduced thermal stability, impaired ability to bind the cofactors
H114F
H115F
H225F
-
the mutant shows reduced activity compared to the wild type enzyme
H310F
-
the mutant shows reduced activity compared to the wild type enzyme
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
A101T
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
E473D
E473Q
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
additional information
A387L
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site-directed mutagenesis, the mutant shows increased Km values for for pyruvate and for 2-oxoisovaleratewere are higher than those of the wild-type Kp-IpdC
A387L
-
site-directed mutagenesis, the mutant shows increased Km values for for pyruvate and for 2-oxoisovalerate are higher than those of the wild-type Kp-IpdC
A143T/T156A/Q367H/N396I/K478R
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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
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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
-
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
-
mutant with abolished activation and reduced Hill coefficient
C221S
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mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6
D28A
-
lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction
D28A
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
D28A
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
D28A
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
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
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
D28N
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type 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
-
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
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
E477Q
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
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
A101T
-
the transcriptome profile analysis of the mutant strain indicates the upregulation of phosphate pathway and pyruvate decarboxylase
-
A101T
-
the transcriptome profile analysis of the mutant strain indicates the upregulation of phosphate pathway and pyruvate decarboxylase
-
E473D
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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
a thermostable, organic solvent stable PDC enzyme variant, PDC-Var. 2, is evolved from the bacterial PDC. The engineered variant shows about 1500fold improved half-life at 75°C and about 5000fold increased half-life in the presence of 9 vol% butanol at 50°C. half-lives of wild-type ApPDC are 57 min, 1.2 min and 10.8 s at 65, 70 and 75°C, respectively. Half-lives of mutant PDC-Var. 2 are 18, 10.7 and 7.3 h at 65, 70 and 75°C, respectively
additional information
generation of enzyme knockout pdc1/pdc2 plants that do not show any obvious phenotype upon visual inspection. But mutant pdc1pdc2 plants show highly reduced growth similar to longtime waterlogged plants. Short-term submergence is more detrimental than long-term waterlogging, growth is severely reduced as a consequence of submergence. ADH1 and PDC1 are expressed in aerobic roots and strongly upregulated by waterlogging and submergence
additional information
generation of enzyme knockout pdc1/pdc2 plants that do not show any obvious phenotype upon visual inspection. But mutant pdc1pdc2 plants show highly reduced growth similar to longtime waterlogged plants. Short-term submergence is more detrimental than long-term waterlogging, growth is severely reduced as a consequence of submergence. ADH1 and PDC1 are expressed in aerobic roots and strongly upregulated by waterlogging and submergence
additional information
generation of enzyme knockout pdc1/pdc2 plants that do not show any obvious phenotype upon visual inspection. But mutant pdc1pdc2 plants show highly reduced growth similar to longtime waterlogged plants. Short-term submergence is more detrimental than long-term waterlogging, growth is severely reduced as a consequence of submergence
additional information
generation of enzyme knockout pdc1/pdc2 plants that do not show any obvious phenotype upon visual inspection. But mutant pdc1pdc2 plants show highly reduced growth similar to longtime waterlogged plants. Short-term submergence is more detrimental than long-term waterlogging, growth is severely reduced as a consequence of submergence
additional information
-
generation of enzyme knockout pdc1/pdc2 plants that do not show any obvious phenotype upon visual inspection. But mutant pdc1pdc2 plants show highly reduced growth similar to longtime waterlogged plants. Short-term submergence is more detrimental than long-term waterlogging, growth is severely reduced as a consequence of submergence. ADH1 and PDC1 are expressed in aerobic roots and strongly upregulated by waterlogging and submergence
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additional information
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generation of enzyme knockout pdc1/pdc2 plants that do not show any obvious phenotype upon visual inspection. But mutant pdc1pdc2 plants show highly reduced growth similar to longtime waterlogged plants. Short-term submergence is more detrimental than long-term waterlogging, growth is severely reduced as a consequence of submergence
-
additional information
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batch and continuous cultivation processes of Candida tropicalis strain TISTR 5306 for ethanol and pyruvate decarboxylase production in fresh longan juice with optimal carbon to nitrogen molar ratio. Method development, effects of C/N molar ratio and sugar composition on microbial growth, ethanol production, and specific PDC activity, evaluation, and growth kinetics, detailed overview. The scores of specific PDC activity are optimal during C/N molar ratios between 15.88 (95.2%) and 21.88 (100%), while further decrease or increase of C/N molar ratios to 9.88 or 39.07 results in the drop of specific PDC activity scores to only 50.2% and 35.3%, respectively
additional information
Candida tropicalis TISTR 5306
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batch and continuous cultivation processes of Candida tropicalis strain TISTR 5306 for ethanol and pyruvate decarboxylase production in fresh longan juice with optimal carbon to nitrogen molar ratio. Method development, effects of C/N molar ratio and sugar composition on microbial growth, ethanol production, and specific PDC activity, evaluation, and growth kinetics, detailed overview. The scores of specific PDC activity are optimal during C/N molar ratios between 15.88 (95.2%) and 21.88 (100%), while further decrease or increase of C/N molar ratios to 9.88 or 39.07 results in the drop of specific PDC activity scores to only 50.2% and 35.3%, respectively
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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
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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
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isobutanol production using strains with variants of Kp-IpdC, overview
additional information
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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
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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
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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
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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
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growth profile and ethanol production in isozyme knockout strains, overview
additional information
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growth profile and ethanol production in isozyme knockout strains, overview
-
additional information
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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
to produce bioethanol from model cyanobacteria such as Synechocystis, a two gene cassette consisting of genes encoding pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are required to transform pyruvate first to acetaldehyde and then to ethanol. Zymobacter palmae pyruvate decarboxylase is less effective than that of Zymomonas mobilis for ethanol production in metabolically engineered Synechocystis sp. PCC6803. The Zppdc gene is combined with the native slr1192 alcohol dehydrogenase gene (adhA) in an attempt to increase ethanol production in the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803 over constructs created with the traditional Zmpdc. Native (Zppdc). Codon optimized (ZpOpdc) versions of the ZpPDC are cloned into a construct where pdc expression is controlled via the psbA2 light inducible promoter from Synechocystis sp. PCC 6803. These constructs are transformed into wild-type Synechocystis sp. PCC 6803 for expression and ethanol production. Ethanol levels are then compared with identical constructs containing the Zmpdc. While strains with the Zppdc (UL071) and ZpOpdc (UL072) constructs do produce ethanol, levels are lower compared to a control strain (UL070) expressing the pdc from Zymomonas mobilis. All constructs demonstrate lower biomass productivity illustrating that the flux from pyruvate to ethanol has a major effect on biomass and ultimately overall biofuel productivity. Thus the utilization of a PDC with a lower Km from Zymobacter palmae unusually does not result in enhanced ethanol production in Synechocystis sp. PCC 6803
additional information
development of a production process of PDC from Zymobacter palmae. The enzyme has been cloned and overexpressed in Escherichia coli, evaluation of the production of recombinant PDC in a bench-scale bioreactor, applying a substrate-limiting fed-batch strategy which leads to a volumetric productivity and a final PDC specific activity of 6942 U/l/h and 3677 U/g DCW (dry cell weight). PDC is purified in fast protein liquid chromatography equipment by ion exchange chromatography. The developed purification process results in 100% purification yield and a purification factor of 3.8
additional information
-
to produce bioethanol from model cyanobacteria such as Synechocystis, a two gene cassette consisting of genes encoding pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are required to transform pyruvate first to acetaldehyde and then to ethanol. Zymobacter palmae pyruvate decarboxylase is less effective than that of Zymomonas mobilis for ethanol production in metabolically engineered Synechocystis sp. PCC6803. The Zppdc gene is combined with the native slr1192 alcohol dehydrogenase gene (adhA) in an attempt to increase ethanol production in the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803 over constructs created with the traditional Zmpdc. Native (Zppdc). Codon optimized (ZpOpdc) versions of the ZpPDC are cloned into a construct where pdc expression is controlled via the psbA2 light inducible promoter from Synechocystis sp. PCC 6803. These constructs are transformed into wild-type Synechocystis sp. PCC 6803 for expression and ethanol production. Ethanol levels are then compared with identical constructs containing the Zmpdc. While strains with the Zppdc (UL071) and ZpOpdc (UL072) constructs do produce ethanol, levels are lower compared to a control strain (UL070) expressing the pdc from Zymomonas mobilis. All constructs demonstrate lower biomass productivity illustrating that the flux from pyruvate to ethanol has a major effect on biomass and ultimately overall biofuel productivity. Thus the utilization of a PDC with a lower Km from Zymobacter palmae unusually does not result in enhanced ethanol production in Synechocystis sp. PCC 6803
-
additional information
-
development of a production process of PDC from Zymobacter palmae. The enzyme has been cloned and overexpressed in Escherichia coli, evaluation of the production of recombinant PDC in a bench-scale bioreactor, applying a substrate-limiting fed-batch strategy which leads to a volumetric productivity and a final PDC specific activity of 6942 U/l/h and 3677 U/g DCW (dry cell weight). PDC is purified in fast protein liquid chromatography equipment by ion exchange chromatography. The developed purification process results in 100% purification yield and a purification factor of 3.8
-
additional information
engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data
additional information
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engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data
additional information
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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
engineered enzyme 5TMA, a PDC expressed in Escherichia coli strain Rosetta, does not show any loss of molar ellipticity, measured by circular dichroism and is stable at 60°C, observed by DIC microscopy. But kinetic stability studies based on activity suggest otherwise: enzyme 5TMA is less stable than wild-type ZmPDC, the parental PDC, in respect to T50_1 h and Tm, at pH 6.5
additional information
acetaldehyde inhibits microbial growth already at millimolar concentrations. Acetaldehyde has no specific membrane permease, its diffusion through the lipid bilayer is slower than that of ethanol, and may represent a serious bottleneck for acetaldehyde producers. It can be improved by moving the acetaldehyde-generating reaction from the cell interior to the periplasmic compartment. Acetaldehyde, when generated in the periplasm and removed from the culture medium by gassing, can be expected to cause less damage to the cell interior, and also, to be less accessible for the cytosolic enzymes, converting it into ethanol or acetate. Engineering of a Zymomonas mobilis strain with acetaldehyde synthesis reaction localized in periplasm for improvement of acetaldehyde production by minimizing its contact with the cell interior and facilitating its removal from the culture. Resulting recombinant strain PeriAc has most of its PDC localized in periplasm and shows a twofold higher acetaldehyde yield than the parent strain. Cell evaluation, overview. It can be used for further improvement by directed evolution. PDC-deficient strains appear to be leaky
additional information
to produce bioethanol from model cyanobacteria such as Synechocystis, a two gene cassette consisting of genes encoding pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are required to transform pyruvate first to acetaldehyde and then to ethanol. Zymobacter palmae pyruvate decarboxylase is less effective than that of Zymomonas mobilis for ethanol production in metabolically engineered Synechocystis sp. PCC6803. The Zppdc gene is combined with the native slr1192 alcohol dehydrogenase gene (adhA) in an attempt to increase ethanol production in the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803 over constructs created with the traditional Zmpdc. Native (Zppdc). Codon optimized (ZpOpdc) versions of the ZpPDC are cloned into a construct where pdc expression is controlled via the psbA2 light inducible promoter from Synechocystis sp. PCC 6803. These constructs are transformed into wild-type Synechocystis sp. PCC 6803 for expression and ethanol production. Ethanol levels are then compared with identical constructs containing the Zmpdc. While strains with the Zppdc (UL071) and ZpOpdc (UL072) constructs do produce ethanol, levels are lower compared to a control strain (UL070) expressing the pdc from Zymomonas mobilis. All constructs demonstrate lower biomass productivity illustrating that the flux from pyruvate to ethanol has a major effect on biomass and ultimately overall biofuel productivity. Thus the utilization of a PDC with a lower Km from Zymobacter palmae unusually does not result in enhanced ethanol production in Synechocystis sp. PCC 6803
additional information
-
engineered enzyme 5TMA, a PDC expressed in Escherichia coli strain Rosetta, does not show any loss of molar ellipticity, measured by circular dichroism and is stable at 60°C, observed by DIC microscopy. But kinetic stability studies based on activity suggest otherwise: enzyme 5TMA is less stable than wild-type ZmPDC, the parental PDC, in respect to T50_1 h and Tm, at pH 6.5
-
additional information
-
acetaldehyde inhibits microbial growth already at millimolar concentrations. Acetaldehyde has no specific membrane permease, its diffusion through the lipid bilayer is slower than that of ethanol, and may represent a serious bottleneck for acetaldehyde producers. It can be improved by moving the acetaldehyde-generating reaction from the cell interior to the periplasmic compartment. Acetaldehyde, when generated in the periplasm and removed from the culture medium by gassing, can be expected to cause less damage to the cell interior, and also, to be less accessible for the cytosolic enzymes, converting it into ethanol or acetate. Engineering of a Zymomonas mobilis strain with acetaldehyde synthesis reaction localized in periplasm for improvement of acetaldehyde production by minimizing its contact with the cell interior and facilitating its removal from the culture. Resulting recombinant strain PeriAc has most of its PDC localized in periplasm and shows a twofold higher acetaldehyde yield than the parent strain. Cell evaluation, overview. It can be used for further improvement by directed evolution. PDC-deficient strains appear to be leaky
-
additional information
-
to produce bioethanol from model cyanobacteria such as Synechocystis, a two gene cassette consisting of genes encoding pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are required to transform pyruvate first to acetaldehyde and then to ethanol. Zymobacter palmae pyruvate decarboxylase is less effective than that of Zymomonas mobilis for ethanol production in metabolically engineered Synechocystis sp. PCC6803. The Zppdc gene is combined with the native slr1192 alcohol dehydrogenase gene (adhA) in an attempt to increase ethanol production in the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803 over constructs created with the traditional Zmpdc. Native (Zppdc). Codon optimized (ZpOpdc) versions of the ZpPDC are cloned into a construct where pdc expression is controlled via the psbA2 light inducible promoter from Synechocystis sp. PCC 6803. These constructs are transformed into wild-type Synechocystis sp. PCC 6803 for expression and ethanol production. Ethanol levels are then compared with identical constructs containing the Zmpdc. While strains with the Zppdc (UL071) and ZpOpdc (UL072) constructs do produce ethanol, levels are lower compared to a control strain (UL070) expressing the pdc from Zymomonas mobilis. All constructs demonstrate lower biomass productivity illustrating that the flux from pyruvate to ethanol has a major effect on biomass and ultimately overall biofuel productivity. Thus the utilization of a PDC with a lower Km from Zymobacter palmae unusually does not result in enhanced ethanol production in Synechocystis sp. PCC 6803
-
additional information
-
engineered enzyme 5TMA, a PDC expressed in Escherichia coli strain Rosetta, does not show any loss of molar ellipticity, measured by circular dichroism and is stable at 60°C, observed by DIC microscopy. But kinetic stability studies based on activity suggest otherwise: enzyme 5TMA is less stable than wild-type ZmPDC, the parental PDC, in respect to T50_1 h and Tm, at pH 6.5
-
additional information
-
acetaldehyde inhibits microbial growth already at millimolar concentrations. Acetaldehyde has no specific membrane permease, its diffusion through the lipid bilayer is slower than that of ethanol, and may represent a serious bottleneck for acetaldehyde producers. It can be improved by moving the acetaldehyde-generating reaction from the cell interior to the periplasmic compartment. Acetaldehyde, when generated in the periplasm and removed from the culture medium by gassing, can be expected to cause less damage to the cell interior, and also, to be less accessible for the cytosolic enzymes, converting it into ethanol or acetate. Engineering of a Zymomonas mobilis strain with acetaldehyde synthesis reaction localized in periplasm for improvement of acetaldehyde production by minimizing its contact with the cell interior and facilitating its removal from the culture. Resulting recombinant strain PeriAc has most of its PDC localized in periplasm and shows a twofold higher acetaldehyde yield than the parent strain. Cell evaluation, overview. It can be used for further improvement by directed evolution. PDC-deficient strains appear to be leaky
-
additional information
-
to produce bioethanol from model cyanobacteria such as Synechocystis, a two gene cassette consisting of genes encoding pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are required to transform pyruvate first to acetaldehyde and then to ethanol. Zymobacter palmae pyruvate decarboxylase is less effective than that of Zymomonas mobilis for ethanol production in metabolically engineered Synechocystis sp. PCC6803. The Zppdc gene is combined with the native slr1192 alcohol dehydrogenase gene (adhA) in an attempt to increase ethanol production in the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803 over constructs created with the traditional Zmpdc. Native (Zppdc). Codon optimized (ZpOpdc) versions of the ZpPDC are cloned into a construct where pdc expression is controlled via the psbA2 light inducible promoter from Synechocystis sp. PCC 6803. These constructs are transformed into wild-type Synechocystis sp. PCC 6803 for expression and ethanol production. Ethanol levels are then compared with identical constructs containing the Zmpdc. While strains with the Zppdc (UL071) and ZpOpdc (UL072) constructs do produce ethanol, levels are lower compared to a control strain (UL070) expressing the pdc from Zymomonas mobilis. All constructs demonstrate lower biomass productivity illustrating that the flux from pyruvate to ethanol has a major effect on biomass and ultimately overall biofuel productivity. Thus the utilization of a PDC with a lower Km from Zymobacter palmae unusually does not result in enhanced ethanol production in Synechocystis sp. PCC 6803
-
additional information
-
engineered enzyme 5TMA, a PDC expressed in Escherichia coli strain Rosetta, does not show any loss of molar ellipticity, measured by circular dichroism and is stable at 60°C, observed by DIC microscopy. But kinetic stability studies based on activity suggest otherwise: enzyme 5TMA is less stable than wild-type ZmPDC, the parental PDC, in respect to T50_1 h and Tm, at pH 6.5
-
additional information
-
acetaldehyde inhibits microbial growth already at millimolar concentrations. Acetaldehyde has no specific membrane permease, its diffusion through the lipid bilayer is slower than that of ethanol, and may represent a serious bottleneck for acetaldehyde producers. It can be improved by moving the acetaldehyde-generating reaction from the cell interior to the periplasmic compartment. Acetaldehyde, when generated in the periplasm and removed from the culture medium by gassing, can be expected to cause less damage to the cell interior, and also, to be less accessible for the cytosolic enzymes, converting it into ethanol or acetate. Engineering of a Zymomonas mobilis strain with acetaldehyde synthesis reaction localized in periplasm for improvement of acetaldehyde production by minimizing its contact with the cell interior and facilitating its removal from the culture. Resulting recombinant strain PeriAc has most of its PDC localized in periplasm and shows a twofold higher acetaldehyde yield than the parent strain. Cell evaluation, overview. It can be used for further improvement by directed evolution. PDC-deficient strains appear to be leaky
-
additional information
-
to produce bioethanol from model cyanobacteria such as Synechocystis, a two gene cassette consisting of genes encoding pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) are required to transform pyruvate first to acetaldehyde and then to ethanol. Zymobacter palmae pyruvate decarboxylase is less effective than that of Zymomonas mobilis for ethanol production in metabolically engineered Synechocystis sp. PCC6803. The Zppdc gene is combined with the native slr1192 alcohol dehydrogenase gene (adhA) in an attempt to increase ethanol production in the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803 over constructs created with the traditional Zmpdc. Native (Zppdc). Codon optimized (ZpOpdc) versions of the ZpPDC are cloned into a construct where pdc expression is controlled via the psbA2 light inducible promoter from Synechocystis sp. PCC 6803. These constructs are transformed into wild-type Synechocystis sp. PCC 6803 for expression and ethanol production. Ethanol levels are then compared with identical constructs containing the Zmpdc. While strains with the Zppdc (UL071) and ZpOpdc (UL072) constructs do produce ethanol, levels are lower compared to a control strain (UL070) expressing the pdc from Zymomonas mobilis. All constructs demonstrate lower biomass productivity illustrating that the flux from pyruvate to ethanol has a major effect on biomass and ultimately overall biofuel productivity. Thus the utilization of a PDC with a lower Km from Zymobacter palmae unusually does not result in enhanced ethanol production in Synechocystis sp. PCC 6803
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additional information
the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
additional information
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
Zymomonas mobilis subsp. pomaceae Barker I
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
Zymomonas mobilis subsp. pomaceae CCUG 17912
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
Zymomonas mobilis subsp. pomaceae DSM 22645
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
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the ABE pathway in Clostridium acetobutylicum strain DSM 792 is modified by overexpressing the pyruvate decarboxylase gene from Zymomonas mobilis under the control of 2 promoters, namely Pferr and Ppta (promoters of genes encoding pyruvate ferredoxin oxidoreductase and phosphotransacetylase). The recombinant strains are designated as DSM 792(pPDC1) and DSM 792(pPDC2). The specific activity of the alcohol dehydrogenases in the pdc-expressing strains is higher than that in the wild-type strain. In batch fermentation experiments, the total ABE production from the recombinant strains DSM 792 (pPDC1) and DSM 792 (pPDC2) is 1.57 and 7.9 g/l, respectively, which is higher when compared to the wild-type ABE production (0.64 g/l) under uncontrolled pH. The alcohol to acetone ratio (BE/A) is 2.28, 2.77, and 5.26 in wild-type, DSM 792 (pPDC1), and DSM 792 (pPDC2), respectively. This suggests that the re-routing of pyruvate by overexpression of the pdc could play a role in the generation of more reducing equivalents towards ethanol and butanol production. Method, overview
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additional information
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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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
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the enzyme is stable at pH 6.5/8.0 for several days, complete activity loss occurs within 2 h at pH 4.0 or 9.0
4.9 - 7.5
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the kcat for native Pdc1 is maximal between pH 6 and pH 6.6, dropping gradually as pH increases to 7.5 and falling rapidly as pH decreases to 4.9
5 - 7
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the enzyme shows no activity loss at pH 5.8-7.0 within 60 h, half-life at pH 4.0 is 2.3 h
5 - 8
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half-life of 80 h at pH 5, half-life of 53 h at pH 7.0, half-life of 13 h at pH 8.0
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 35
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half-life of 235 h at 20°C, half-life of 78 h at 30°C, half-life of 62 h at 35°C
30 - 60
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half-life of 150 h at 30°C, 40 h at 40°C, 10 h at 50°C, and 0.4 h at 60°C
30 - 70
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half-life of 144 h at 30°C, 34 h at 40°C, 12 h at 50°C, 2 h at 60°C, and 0.4 h at 70°C
4
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about 40% of the activity is lost after 5 days incubation at 4°C (without stirring)
40
42
in presence of 1 mM thiamine diphosphate, 1 mM Mg2+, pH 6.5, stable up to
45 - 65
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the activity of native Pdc1 decreases with increasing temperature from 45°C and is completely abolished at 65°C, the temperature at which half of the native Pdc1 activity is irreversibly lost in 5 min is at 52.6°C
50
52
55
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the enzyme retains 20% of activity after 30 min at 55°C. The half-life is 12 h at 50°C and 2 h at 60°C
55 - 80
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approximately 40% and 30% enzyme activity is retained after 30 min and 1 h at 65°C, respectively. The native enzyme is stable for 5 min at 55°C but completely inactivated by incubating for 3 min at 80°C
60
65
65 - 75
half-lives of wild-type ApPDC are 57 min, 1.2 min and 10.8 s at 65, 70 and 75°C, respectively. Half-lives of mutant PDC-Var. 2 are 18, 10.7 and 7.3 h at 65, 70 and 75°C, respectively
80
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
half-life of pyruvate decarboxylase activity 2 h, of pyruvate ferredoxin oxidoreductase activity 3 h
40
1 h, 73.2% residual activity, isoform PDC, 93.2% residual activity, isoform PDC II
50
1 h, 23.9% residual activity, isoform PDC, 43.1% residual activity, isoform PDC II
60
the enzyme shows a half-life of18 min at 60°C
60
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at temperatures of or below 60°C the enzyme retains 30% of the initial activity at 65°C after an h of incubation
60
1 h, 3% residual activity, isoform PDC, 2.7% residual activity, isoform PDC II
65
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purified recombinant enzyme, 40% enzyme activity remain after 30 min
65
the enzyme retains 80% activity after incubation at 65°C for 30 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1 mM thiamine diphosphate is sufficient to keep the enzyme stable and active in potassium phosphate buffer for several days
6°C, 20 mM MOPS, pH 7, half-life of enzyme is 138 h, addition of benzaldehyde emulsion causes rapid deactivation. Glycerol does not protect, but pyruvate does
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central role of the beta domain in stabilizing the overall structure
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half-life of 3 days for both crude enzyme extract and 2 days for whole cell biomass preparations in presence of 50 mM benzaldehyde at 22°C
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half-life of 5 days for both crude enzyme extract and 3.5 days for whole cell biomass preparations in presence of 50 mM benzaldehyde at 22°C
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half-life of 7 days for both crude enzyme extract and whole cell biomass preparations in presence of 50 mM benzaldehyde at 22°C, half-life of nearly 2 weeks for crude enzyme extract and slightly longer for whole cell biomass in absence of benzaldehyde
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low stability in the isolated state, less stable than PDC from Zymomonas mobilis
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more stable than PDC from Saccharomyces cerevisiae, stirring deactivates significantly
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retains about 50% of activity in buffer supplemented with 2 M NaCl or KCl, retain 20% of activity in 4 M salt buffer
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the enzyme in phosphate buffer pressurized with CO2 up to 9 MPa for 1 h at 35°C loses most of its activity. Although the residual activity is higher in MES buffer than in phosphate buffer, deactivation cannot be prevented. With 0.7 M glycerol, the residual activity is double that without additives, and with 1-1.2 M trehalose, the residual activity is 1.5times that without additives. The stability of the enzyme is improved dramatically by immobilization onto the ion-exchange polymer Mukouyama 2000, the biocatalytic activity is fully retained even after treatment at 11 MPa. The stability of the enzyme immobilized on Toyonite-200 is lower than that of free enzyme
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the highest enzyme activity is in glucose, followed by glycerol, while there is negligible activity on ethanol and methanol as growth medium
with about 1 mM pyruvate, native Pdc1 only reaches a stable reaction rate after exposure to pyruvate for 1 min, the N-terminal His tag has no influence on activity of native Pdc1
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0.1 mM thiamine diphosphate is sufficient to keep the enzyme stable and active in potassium phosphate buffer for several days
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0.1 mM thiamine diphosphate is sufficient to keep the enzyme stable and active in potassium phosphate buffer for several days
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0.1 mM thiamine diphosphate is sufficient to keep the enzyme stable and active in potassium phosphate buffer for several days
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the highest enzyme activity is in glucose, followed by glycerol, while there is negligible activity on ethanol and methanol as growth medium
the highest enzyme activity is in glucose, followed by glycerol, while there is negligible activity on ethanol and methanol as growth medium
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
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treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity are extremely oxygen sensitive, 50% loss of activity upon exposure to air at room temperature within 15 min
oxygen-sensitive enzyme, the t1/2 for the enzyme activity in 50 mM Tris-HCl, pH7.8 containing 2 mM sodium dithionite and 2 mM DTT is approximately 30 min
726840
PDC shows two phases when determined aerobically: a fast phase in which the enzyme loses half of its activity within 15 to 20 minutes, and the second phase which is comparatively slow due to slow denaturation of enzymatic protein. Half-life of 20 minutes after exposure to O2.
763539
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity are extremely oxygen sensitive, 50% loss of activity upon exposure to air at room temperature within 15 min
736379
both pyruvate decarboxylase and pyruvate ferredoxin oxidoreductase activity are extremely oxygen sensitive, 50% loss of activity upon exposure to air at room temperature within 15 min
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
736379
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or -80°C, pH 6.0, 1 mM thiamine diphosphate, 1 mM MgSO4, minimum protein concentration 0.2 mg/ml, stable for several months
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-20°C, concentrated PDC, buffered solution containing thiamine diphosphate and MgSO4, several months, stable
-70°C, 10 mM PIPES at pH 6.5 with 1 mM dithiothreitol, 1 mM MgCl2, and 0.1 mM thiamine diphosphate, several weeks, no loss of activity
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half-life of 3 days for crude enzyme extract and less than 1 day for whole cell biomass in absence or presence of benzaldehyde at 22°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
HisTrap column chromatography, Fractogel EMD TMAE 650S gel filtration, and Superdex 200 gel filtration
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native enzyme 6.3fold to homogeneity from cell-free extract by anion exchange chromatography, hydroxyapatite chromatography, adsorption chromatography, and gel filtration, followed by ultrafiltration. All buffers contain 1 mM TPP and 1 mM MgSO4
native enzyme by acetone precipitation, ammonium sulfate fractionation, and gel filtration to over 95% homogeneity
native enzyme by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography to over 95% homogeneity
native isozyme 17fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography
native isozyme 22fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography
partial
partially purified, ammonium sulfate precipitation and phenyl Sepharose column chromatography
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purified enzyme shos a brownish colour characteristic of iron-sulfur containing proteins
purified enzyme shows a brownish colour characteristic of iron-sulfur containing proteins
V9NGI4; V9NFX1; V9NGQ2; V9NHA1
recombinant enzyme PDC 3.8fold to homogeneity from Zymomonas palmae by ammonium sulfate fractionation, ion exchange chromatography, and desalting gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography
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recombinant mutants D28A and His6-tagged E477Q, the latter on a talon resin
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recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
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W412F and W412A mutant PDC, expressed in Escherichia coli, W412A is purified as apoenzyme
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wild-type, E91A, E91D and E91Q mutant PDC, expressed in Escherichia coli, mutants are purified as apoenzymes
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 pyruvate decarboxylase genes diverge significantly from one another and from other yeast pyruvate decarboxylase genes
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Geobacillus thermoglucosidasius
expressed in Hansenula polymorpha
expressed in pyruvate decarboxylase-deficient Saccharomyces cerevisiae strain D452-2
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expression in Escherichia coli
expression in Saccharomyces cerevisiae, in a decarboxylase-negative pdc1Delta,pdc5Delta, pdc6Delta, aro10Delta background
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 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 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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fused with alcohol dehydrogenase and expressed in Escherichia coli JM109 cells
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gene ipdC, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
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gene pdc, cloning in Escherichia coli TOP10 cells and functional recombinant transgenic expression in Clostridium acetobutylicum strain DSM 792, co-expression of genes pdc and adh from Zymomonas mobilis
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, construction of periplasmically expressed pyruvate decarboxylase, carrying the 35 amino acid periplasmic signal sequence of Zymomonas mobilis gluconolactonase (EC 3.1.1.17, UniProtKB ID Q01578) attached to its N-terminus, a 134 bp primer SglucPdc_fwd, subcloning in Escherichia coli strain JM109
gene pdc, recombinant expression in an acetolactate-synthase-deficient mutant of Klebsiella pneumoniae
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gene pdc, recombinant expression of enzyme PDC in Escherichia coli strain M15 under control of the lac promoter using plasmid pJAM3440
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
gene zmpdc, recombinant expression of codon optimized gene in Escherichia coli strain BL21(DE3), transgenic expression in Synechocystis sp. PCC 6803
gene zppdc, recombinant expression of codon optimized gene in Escherichia coli strain BL21(DE3), transgenic expression in Synechocystis sp. PCC 6803
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
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
expressed in Escherichia coli BL21(DE3)pLysS cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-ketoisovalerate decarboxylase (kivD), BCAA-specific aminotransferase (bcaT) and C-S lyase (yjtE) gene expressions increase markedly by both isoleucine and valine starvation
both PDC1 and PDC2 are strongly upregulated under hypoxia
both PDC1 and PDC2 are strongly upregulated under hypoxia. PDC1 is strongly upregulated by waterlogging and submergence in aerobic roots
expression of both PDC1 and PDC2 is strongly upregulated under low oxygen
for PDC, the level of transcripts remain quantitatively constant in all fruit maturity stages
gene expression is not induced by 2,4-dichlorophenoxyacetic acid treatment
gene PDC3 is not regulated by low-oxygen stress
gene PDC4 is not regulated by low-oxygen stress
isoform PDC1, PDC2 and PDC3 show striking expressional responses in leaves and bark to drought, low temperature and high temperature stresses
isoleucine starvation increases 4fold the Kivd activity compared to cells grown in chemically defined medium with casitone as nitrogen source. Regulation of expression is at the transcription level, probably mediated by CodY
PDC4 expression is down-regulated as the degree of tapping panel dryness increases
PDC4 expression is induced by tapping, with transcripts showing a rapid increase (150fold) during the first seven tappings, and PDC4 shows a rapid increase in expression after wounding treatment
the expression of both isoforms PDC1 and PDC2 is strongly up-regulated under low oxygen
the expression of isoform PDC1 is enhanced by D-glucose
alpha-ketoisovalerate decarboxylase (kivD), BCAA-specific aminotransferase (bcaT) and C-S lyase (yjtE) gene expressions increase markedly by both isoleucine and valine starvation
alpha-ketoisovalerate decarboxylase (kivD), BCAA-specific aminotransferase (bcaT) and C-S lyase (yjtE) gene expressions increase markedly by both isoleucine and valine starvation
-
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both PDC1 and PDC2 are strongly upregulated under hypoxia. PDC1 is strongly upregulated by waterlogging and submergence in aerobic roots
both PDC1 and PDC2 are strongly upregulated under hypoxia. PDC1 is strongly upregulated by waterlogging and submergence in aerobic roots
-
-
expression of both PDC1 and PDC2 is strongly upregulated under low oxygen
expression of both PDC1 and PDC2 is strongly upregulated under low oxygen
-
-
gene PDC3 is not regulated by low-oxygen stress
gene PDC4 is not regulated by low-oxygen stress
isoleucine starvation increases 4fold the Kivd activity compared to cells grown in chemically defined medium with casitone as nitrogen source. Regulation of expression is at the transcription level, probably mediated by CodY
isoleucine starvation increases 4fold the Kivd activity compared to cells grown in chemically defined medium with casitone as nitrogen source. Regulation of expression is at the transcription level, probably mediated by CodY
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation of apoenzyme with MgCl2 is achieved by incubation of dialyzed enzyme with 1 mM thiamine diphosphate and increasing concentrations of MgCl2
-
study of subunit dissociation into two types of dimers depending on the experimental conditions and their reassociation
-
unfolding and folding kinetics after treatment with urea, reactivation study in terms of dependence on different conditions and additives, reactivation of homomeric PDC requires both refolding to monomers and their correct association to enzymatically active dimers or tetramers
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
synthesis
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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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
-
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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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
-
engineered enzyme mutants are useful for synthesis of both enantiomers of alpha-ketols and acetolactates with good enantiomeric excess, overview
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
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
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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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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
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
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
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
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
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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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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
pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
synthesis
pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
synthesis
pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
synthesis
pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
synthesis
pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
synthesis
PDC is a very powerful tool in the enzymatic synthesis of chiral amines by combining it with transaminases when alanine is used as amine donor. For its use in biocatalysis, its production and the downstream processing on scale are optimized in a production process of PDC from Zymobacter palmae
synthesis
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pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
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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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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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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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pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
-
synthesis
Nakaseomyces glabratus ATCC 2001
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pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
-
synthesis
-
pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
-
synthesis
-
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
-
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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pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
-
synthesis
Nakaseomyces glabratus JCM 3761
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pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
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synthesis
Nakaseomyces glabratus NBRC 0622
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pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
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synthesis
Nakaseomyces glabratus NRRL Y-65
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pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
-
synthesis
-
pyruvate decarboxylase (PDC) is a key enzyme for the production of ethanol at high temperatures and for cell-free butanol synthesis
-
synthesis
-
PDC is a very powerful tool in the enzymatic synthesis of chiral amines by combining it with transaminases when alanine is used as amine donor. For its use in biocatalysis, its production and the downstream processing on scale are optimized in a production process of PDC from Zymobacter palmae
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Release 2026.1 (March 2026)
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