Information on EC 4.1.1.1 - Pyruvate decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.1.1.1
-
RECOMMENDED NAME
GeneOntology No.
Pyruvate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
-
-
-
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalytic mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalytic mechanism, catalyzes the carboligation of 2 aldehydes as side reaction, mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
mechanism, catalyzes carboligation as side reaction
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalytic and kinetic mechanism, catalyzes carboligation as side reaction
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalytic mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions, thermodynamic data
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalytic mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
reaction mechanism, overview
-
a 2-oxo carboxylate = an aldehyde + CO2
show the reaction diagram
catalytic mechanism
Kluyveromyces lactis JA-6
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboligation
-
-
carboligation
-
-
carboligation
Candida tropicalis LU57, Cyberlindnera jadinii UNSW, Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
-
-
decarboxylation
-
-
-
-
decarboxylation
-
-
PATHWAY
KEGG Link
MetaCyc Link
3-methylbutanol biosynthesis
-
acetaldehyde biosynthesis I
-
acetaldehyde biosynthesis II
-
acetoin biosynthesis III
-
Biosynthesis of secondary metabolites
-
chitin degradation to ethanol
-
Glycolysis / Gluconeogenesis
-
leucine degradation III
-
long chain fatty acid ester synthesis for microdiesel production
-
Metabolic pathways
-
pyruvate fermentation to acetate VIII
-
pyruvate fermentation to ethanol II
-
SYSTEMATIC NAME
IUBMB Comments
2-oxo-acid carboxy-lyase (aldehyde-forming)
A thiamine-diphosphate protein. Also catalyses acyloin formation.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8-10 nm cytoplasmic filament-associated protein
-
-
-
-
alpha-Carboxylase
-
-
-
-
alpha-Keto acid carboxylase
-
-
-
-
Decarboxylase, pyruvate
-
-
-
-
GPDC1
Q9FVE1
-
KlPDC
Kluyveromyces lactis JA-6
-
-
-
P59NC
-
-
-
-
PDC
-
-
-
-
PDC
Acetobacter pasteurianus NCIB8618
Q8L388
-
-
PDC
Candida tropicalis LU57
-
-
-
PDC
Cyberlindnera jadinii UNSW
-
;
-
PDC
Cyberlindnera jadinii UNSW70940
-
-
-
PDC
Kluyveromyces lactis CBS 2359
-
-
-
PDC
Kluyveromyces marxianus UNSW 510700
-
-
-
PDC
B0ZS79
-
PDC
Q8NK64, Q8NK65
-
PDC
Saccharomyces cerevisiae UNSW
-
-
-
PDC
Q93EN4
-
PDC
Sarcina ventriculi Goodsir
Q93EN4
-
-
PDC
Q9FVE1
-
PDC
P06672
-
PDC
Zymomonas mobilis ZM4
-
-
-
PDC I
Q6FJA3
-
PDC I
Candida glabrata IFO005
Q6FJA3
-
-
PDC II
Q6FJA3
-
PDC II
Candida glabrata IFO005
Q6FJA3
-
-
PDC1
-
sulfur-rich pyruvate decarboxylase
Pdc1p
-
major isozyme of pyruvate decarboxylase
Pdc6
-
sulfur-poor pyruvate decarboxylase, third minor isozyme of pyruvate decarboxylase
POR
-
bifunctional enzyme that catalyzes both the oxidative and nonoxidative decarboxylation of pyruvate
pyruvamide-activated yeast pyruvate decarboxylase
-
-
pyruvate decarboxylase
-
-
pyruvate decarboxylase 1
-
-
Pyruvic decarboxylase
-
-
-
-
yeast pyruvate decarboxylase
-
-
ZbPDC
Zygosaccharomyces bisporus CBS 702
Q9UUT6
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-04-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain NCIB8618, i.e. ATCC 12874
SwissProt
Manually annotated by BRENDA team
Acetobacter pasteurianus NCIB8618
strain NCIB8618, i.e. ATCC 12874
SwissProt
Manually annotated by BRENDA team
ecotype C24
Q96536
SwissProt
Manually annotated by BRENDA team
pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
-
-
Manually annotated by BRENDA team
strain IFO005, isoforms PDC I and PDC II
Swissprot
Manually annotated by BRENDA team
Candida glabrata IFO005
strain IFO005, isoforms PDC I and PDC II
Swissprot
Manually annotated by BRENDA team
strain LU57
-
-
Manually annotated by BRENDA team
Candida tropicalis LU57
strain LU57
-
-
Manually annotated by BRENDA team
Citrus sp.
-
-
-
Manually annotated by BRENDA team
strain UNSW 70940
-
-
Manually annotated by BRENDA team
strain UNSW70940
-
-
Manually annotated by BRENDA team
Cyberlindnera jadinii UNSW
strain UNSW 70940
-
-
Manually annotated by BRENDA team
Cyberlindnera jadinii UNSW70940
strain UNSW70940
-
-
Manually annotated by BRENDA team
cultivars Jewel and Cavendish
-
-
Manually annotated by BRENDA team
gene product Fapdc1, induced during fruit ripening
Swissprot
Manually annotated by BRENDA team
gene product Fapdc3, constitutively expressed in all tissues studied
-
-
Manually annotated by BRENDA team
single gene
SwissProt
Manually annotated by BRENDA team
strain CBS 2359
-
-
Manually annotated by BRENDA team
strain JA-6
-
-
Manually annotated by BRENDA team
Kluyveromyces lactis CBS 2359
strain CBS 2359
-
-
Manually annotated by BRENDA team
Kluyveromyces lactis JA-6
strain JA-6
-
-
Manually annotated by BRENDA team
strain UNSW 510700
-
-
Manually annotated by BRENDA team
Kluyveromyces marxianus UNSW 510700
strain UNSW 510700
-
-
Manually annotated by BRENDA team
Kluyveromyces sp.
-
-
-
Manually annotated by BRENDA team
isoforms Pdc11, Pdc12, Pdc13, overall enzyme activity is enhanced by glucose and oxygen limitation
-
-
Manually annotated by BRENDA team
cultivar Pink Lady
-
-
Manually annotated by BRENDA team
variant Samsun
-
-
Manually annotated by BRENDA team
no activity in Malassezia pachydermatis
-
-
-
Manually annotated by BRENDA team
no activity in Rhodomicrobium vannielii
-
-
-
Manually annotated by BRENDA team
no activity in Rhodopseudomonas sphaeroides
-
-
-
Manually annotated by BRENDA team
no activity in Rhodospirillum rubrum
-
-
-
Manually annotated by BRENDA team
cultivar Pusa Basmati 1, genes pdc1 and pdc2, pdc gene family
Uniprot
Manually annotated by BRENDA team
isoform Pdc3
-
-
Manually annotated by BRENDA team
pollen-specific isoform Pdc2
-
-
Manually annotated by BRENDA team
3 isoenzymes; cv. Miko
-
-
Manually annotated by BRENDA team
cultivar Modesto
UniProt
Manually annotated by BRENDA team
isozyme 1, gene pdcA; isozyme 1 encoded by gene pdcA
SwissProt
Manually annotated by BRENDA team
isozyme 2, gene pdcB; isozyme 2 encoded by gene pdcB
Q8NK64
SwissProt
Manually annotated by BRENDA team
Rhodopseudomonas palustris Q
strain Q
-
-
Manually annotated by BRENDA team
haploid strain expressing only one of three structural genes for pyruvate decarboxylase, PDC1
-
-
Manually annotated by BRENDA team
more than one gene
SwissProt
Manually annotated by BRENDA team
recombinant homomeric, alpha-only, PDC1
-
-
Manually annotated by BRENDA team
strain S288c
-
-
Manually annotated by BRENDA team
strain UNSW 102200
-
-
Manually annotated by BRENDA team
strain WS34/70
-
-
Manually annotated by BRENDA team
strains S288C, YPH98, and W303-1A
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae UNSW
strain UNSW 102200
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae WS34/70
strain WS34/70
-
-
Manually annotated by BRENDA team
gene pdc
-
-
Manually annotated by BRENDA team
strain Goodsir, ATCC 55887
SwissProt
Manually annotated by BRENDA team
Sarcina ventriculi Goodsir
strain Goodsir, ATCC 55887
SwissProt
Manually annotated by BRENDA team
vatiant Desiree
-
-
Manually annotated by BRENDA team
activity in metronidazole- or iron-restricted cells is 20-30 times higher than in metronidazole-sensitive strain
-
-
Manually annotated by BRENDA team
cv. Perlette, grafted on 140-R root stock, grape
SwissProt
Manually annotated by BRENDA team
i.e. Candida pelliculosa or Hansenula anomala, diploid type strain NRRL-Y-366, haploid strain NRRL-Y-366-8, gene pdc1
SwissProt
Manually annotated by BRENDA team
strain CBS 702
SwissProt
Manually annotated by BRENDA team
Zygosaccharomyces bisporus CBS 702
strain CBS 702
SwissProt
Manually annotated by BRENDA team
expression in Lactococcus lactis
-
-
Manually annotated by BRENDA team
strain DSMZ 10491
-
-
Manually annotated by BRENDA team
expression in Haloferax volcanii, growth-phase dependent decrease in amount of enzyme protein
-
-
Manually annotated by BRENDA team
wild type and mutant enzymes E50D, E50Q, V111A, H113Q, H114Q, D440N, D440T, D440G, D440E, E449D, N467Q, N467D, W487L, F496I, F496H
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-keto-4-methylhexanoic acid
3-methylpentanal + CO2
show the reaction diagram
-
-
-
-
?
2-ketobutanoic acid
propanal + CO2
show the reaction diagram
-
-
-
-
?
2-ketobutyrate
?
show the reaction diagram
P06672
lower activity than with pyruvate
-
?
2-ketobutyric acid
propanal + CO2
show the reaction diagram
-
-
-
-
?
2-ketohexanoic acid
pentanal + CO2
show the reaction diagram
-
-
-
-
?
2-ketopentanoic acid
butanal + CO2
show the reaction diagram
-
-
-
-
?
2-ketovalerate
?
show the reaction diagram
P06672
lower activity than with pyruvate
-
?
2-oxo-4-phenylbutanoic acid
3-phenylpropanal + CO2
show the reaction diagram
-
-
-
-
?
2-oxo-4-phenylbutanoic acid
?
show the reaction diagram
-
-
-
-
?
2-oxo-5-phenylpentanoic acid
4-phenylbutanal + CO2
show the reaction diagram
-
-
-
-
?
2-oxo-5-phenylpentanoic acid
?
show the reaction diagram
-
-
-
-
?
2-Oxobutanoate
?
show the reaction diagram
-
-
-
-
-
2-oxobutanoic acid
propanal + CO2
show the reaction diagram
-
-
-
-
?
2-oxobutanoic acid
?
show the reaction diagram
-
-
-
-
?
2-oxohexanoic acid
pentanal + CO2
show the reaction diagram
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
2-oxohexanoic acid
n-pentanal + CO2
show the reaction diagram
-
-
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
show the reaction diagram
Q684J7
22.7% of the activity with 2-oxoisovalerate
-
-
?
2-Oxoisopentanoate
?
show the reaction diagram
-
-
-
-
-
2-oxoisovalerate
2-methylpropanal + CO2
show the reaction diagram
Q684J7
-
-
-
?
2-oxomethylthiobutyrate
?
show the reaction diagram
Q684J7
7.2% of the activity with 2-oxoisovalerate
-
-
?
2-oxomethylvalerate
?
show the reaction diagram
Q684J7
16.7% of the activity with 2-oxoisovalerate
-
-
?
2-oxooctanoic acid
?
show the reaction diagram
-
-
-
-
?
2-oxooctanoic acid
n-hexanal + CO2
show the reaction diagram
-
-
-
-
?
2-Oxopentanoate
?
show the reaction diagram
-
-
-
-
-
2-oxopentanoic acid
butanal + CO2
show the reaction diagram
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
2-oxopentanoic acid
?
show the reaction diagram
-
-
-
-
?
2-oxopentanoic acid
n-butanal + CO2
show the reaction diagram
-
-
-
-
?
3-(1H-indol-3-yl)-2-oxopropanoic acid
1H-indol-3-ylacetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
3-(1H-indol-3-yl)-2-oxopropanoic acid
?
show the reaction diagram
-
-
-
-
?
3-fluoro-2-oxopropanoic acid
?
show the reaction diagram
-
-
-
-
?
3-fluoro-2-oxopropanoic acid
fluoroacetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
3-Fluoropyruvate
acetate + F- + CO2
show the reaction diagram
-
decarboxylation is followed by release of F-
-
-
3-Hydroxypyruvate
Glycolaldehyde + CO2
show the reaction diagram
-
-
-
-
3-Hydroxypyruvate
Glycolaldehyde + CO2
show the reaction diagram
-
-
-
-
-
3-methyl-2-oxobutanoate
?
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxopentanoic acid
?
show the reaction diagram
-
-
-
-
?
3-phenylpyruvate
2-phenylethanal + CO2
show the reaction diagram
Q684J7
8.8% of the activity with 2-oxoisovalerate
-
-
?
4-methyl-2-oxohexanoic acid
3-methylpentanal + CO2
show the reaction diagram
-
-
-
-
?
4-methyl-2-oxohexanoic acid
?
show the reaction diagram
-
-
-
-
?
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
show the reaction diagram
-
-
-
-
?
4-methyl-2-oxopentanoic acid
?
show the reaction diagram
-
-
-
-
?
a 2-oxo acid
an aldehyde + CO2
show the reaction diagram
-
-
-
-
?
acetaldehyde + acetaldehyde
acetoin
show the reaction diagram
-
carboligation of 2 aldehydes as a side reaction of PDC
-
?
acetaldehyde + acetaldehyde
(S)-acetoin + ?
show the reaction diagram
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
show the reaction diagram
-
carboligation of 2 aldehydes as a side reaction of PDC, high carboligase activity, more active than PDC from Zymomonas mobilis
(R)-phenylacetylcarbinol
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
show the reaction diagram
-
carboligation of 2 aldehydes as a side reaction of PDC, less active than PDC from Saccharomyces cerevisiae
(R)-phenylacetylcarbinol
?
acetaldehyde + benzaldehyde
(1R)-phenylacetylcarbinol
show the reaction diagram
-
-
-
-
-
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
-
-
-
?
acetylphosphinate
?
show the reaction diagram
-
-
-
-
?
benzaldehyde + acetaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
-
reaction proceeds under in vitro assay conditions, colorimetric assay based on reaction
-
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol
show the reaction diagram
-
-
transformation is enhanced by maintenance of neutral pH-value
-
?
benzaldehyde + pyruvate
(1R)-phenylacetylcarbinol
show the reaction diagram
-
-
-
-
ir
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
show the reaction diagram
Cyberlindnera jadinii, Cyberlindnera jadinii UNSW70940
-
-
-
-
ir
Benzoylformate
Benzaldehyde + CO2
show the reaction diagram
-
substrate only for mutant mutant I472A
-
-
?
beta-hydroxypyruvate
2,4-dihydroxymethyl-3-oxo-butanoic acid
show the reaction diagram
-
D28A YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
beta-hydroxypyruvate
glycolaldehyde
show the reaction diagram
-
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
1,3,4-trihydroxy-2-butanone
show the reaction diagram
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
fluoropyruvate
?
show the reaction diagram
-
-
-
?
oxo(phenyl)acetic acid
benzaldehyde + CO2
show the reaction diagram
-
-
-
-
?
oxo(phenyl)acetic acid
?
show the reaction diagram
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
show the reaction diagram
Zygosaccharomyces bisporus, Zygosaccharomyces bisporus CBS 702
Q9UUT6
-
-
?
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
show the reaction diagram
Zygosaccharomyces bisporus, Zygosaccharomyces bisporus CBS 702
Q9UUT6
enzyme catalyzes a carboligation as side reaction
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
r
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
P06672
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Citrus sp.
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
A2XFI3, -
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Kluyveromyces sp., Hanseniaspora uvarum
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q9FVE1, -
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q96536
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q8L388
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q9UUT6
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q6FJA3
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q659I2, -
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q8NK64, Q8NK65
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q12629
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
P06169
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
B0ZS79, -
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
plus acetoin
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
plus racemic acetoin
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
first enzyme in a branch of glycolysis that converts pyruvate to ethanol
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
3-4% acetoin side product
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q93EN4
nonoxidative decarboxylation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
mechanism
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
mechanism
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
only the undissociated pyruvic acid acts as the substrate
-
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
catalytic mechanism
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
4 active sites in the tetramer, enzyme structure
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
active site structure, catalytic mechanism
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
alternating sites mechanism
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
P06672
C-terminal region occludes the active site, enzyme structure, catalytic cycle, active site closure is required for decarboxylation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
catalytic cycle, 3 domains: a diphosphate-binding domain, a pyrimidine-binding domain and a regulatory domain, model for enzyme regulation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
catalytic mechanism, acetaldehyde is produced by protonation of the key C2alpha-carbanion/enamine intermediate
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
catalytic mechanism, contains catalytic and regulatory pyruvate binding site
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
detailed mechanism
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
detailed mechanism with roles for the active center acid-base groups D28, E477, H114 and H115, catalytic cycle, mechanistic model of the reaction, alternating sites model
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
detailed mechanism, catalytic cycle, alternating sites mechanism based on tight communication between active sites of the functional dimer, with the ionizable residues D28, E477 and H115 likely to be important in creating this communication, enzyme exists in three conformations, one inactive and two active forms, enzyme structure
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
H113 is involved in substrate binding and mediates the opening and closing of the active site by ion pairing with the carboxyl group of pyruvate
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
nonoxidative decarboxylation, main reaction
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q9UUT6
key enzyme in alcoholic fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
catalyzes the penultimate step in ethanol fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q93EN4
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
enzyme within the glycolytic pathway in fermenting cells
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
enzyme within the glycolytic pathway in fermenting cells
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q96536
ethanol fermentation pathway, involved in anaerobic metabolism
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q9FVE1, -
involved in the enhancement of ethanol production in berries, but not the limiting factor
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q8L388
key enzyme for the oxidative metabolism of lactic acid
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
key role in the alcoholic fermentation process
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
penultimate step in the alcoholic fermentation process
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
penultimate step of alcohol fermentation
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q659I2, -
enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
A2XFI3, -
Pdc is involved in the operation of ethanolic fermentation pathway that appears to correlate to an extent with anoxia tolerance in plants, overview
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q12629
catalytic cycle, overview
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
P06169
catalytic cycle, overview
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80C (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 (80C)
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Kluyveromyces lactis CBS 2359
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Cyberlindnera jadinii UNSW
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Zymomonas mobilis ZM4
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Sarcina ventriculi Goodsir
Q93EN4
nonoxidative decarboxylation, during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Candida tropicalis LU57
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Kluyveromyces lactis JA-6
-
catalytic mechanism, contains catalytic and regulatory pyruvate binding site, key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Saccharomyces cerevisiae WS34/70
-
4 active sites in the tetramer, enzyme structure, penultimate step in the alcoholic fermentation process
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Kluyveromyces marxianus UNSW 510700
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Rhodopseudomonas palustris Q
-
-
plus acetoin
-
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Saccharomyces cerevisiae UNSW
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Candida glabrata IFO005
Q6FJA3
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Zygosaccharomyces bisporus CBS 702
Q9UUT6
-, key enzyme in alcoholic fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Cyberlindnera jadinii UNSW70940
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Acetobacter pasteurianus NCIB8618
Q8L388
-, key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate
ethanal + CO2
show the reaction diagram
Q684J7
0.6% of the activity with 2-oxoisovalerate
-
-
?
pyruvate
(S)-acetolactate + CO2
show the reaction diagram
-
D28A YPDC variant, not E477Q YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
-
carboligation reaction
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
i.e. 3-hydroxy-2-butanone, formation of the (R)- and the (S)-enantiomers
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
Cyberlindnera jadinii UNSW
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
Candida tropicalis LU57, Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
-, stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
carboligation reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
Cyberlindnera jadinii UNSW
-
-, stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
Cyberlindnera jadinii UNSW, Candida tropicalis LU57, Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + phenylacetaldehyde
3-hydroxy-4-phenyl-butan-2-one + CO2
show the reaction diagram
Q9UUT6
enzyme catalyzes a carboligation as side reaction
-
?
Pyruvic acid
Acetaldehyde + CO2
show the reaction diagram
-
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
-
-
?
indole-3-pyruvate
2-(indol-3-yl)-ethanal + CO2
show the reaction diagram
Q684J7
0.1% of the activity with 2-oxoisovalerate
-
-
?
additional information
?
-
-
the role of the protein component of pyruvate decarboxylase in the mechanism of substrate activation
-
-
-
additional information
?
-
-
catalyzes also carboligase reactions in which the central enamine intermediate reacts with acetaldehyde or pyruvate, instead of the usual proton electrophile, resulting in the formation of acetoin and acetolactate, respectively, typically 1% of the total reaction, stereochemistry of products
-
?
additional information
?
-
-
enzyme catalyzes a carboligase reaction as side reaction forming acetoin and acetolactate
-
?
additional information
?
-
-
enzyme catalyzes also a carboligation as side reaction producing acetoin and acetolactate, mechanism, not: pyruvamide
-
?
additional information
?
-
Q9UUT6
nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
-
?
additional information
?
-
-
not: pyruvamide
-
?
additional information
?
-
-
not: pyruvamide
-
?
additional information
?
-
-
oxidative diversion of the decarboxylation of pyruvate by 2,6-dichlorophenolindophenol, which traps a carbanionic intermediate and diverts the product from acetaldehyde to acetate, kinetics
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
-
additional information
?
-
-
key enzyme in ethanol formation
-
-
-
additional information
?
-
-
key enzyme in alcoholic fermentation
-
-
-
additional information
?
-
-
pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
-
-
-
additional information
?
-
-
key enzyme in glycolytic pathway to ethanol
-
-
-
additional information
?
-
-
involved in a pathway in which NAD+ is regenerated under anaerobic conditions
-
-
-
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
-
additional information
?
-
-
one of the key enzymes involved in fermentation process
-
-
-
additional information
?
-
-
critical enzyme in a pollen-specific pathway to bypass pyruvate dehydrogenase enzymes and maintain biosynthetic capacity and energy production under the unique conditions prevailing during pollen-pistil interaction
-
-
-
additional information
?
-
-
involved in aerobic fermentation in mature pollen
-
-
-
additional information
?
-
-, Q8W2B3
involved in fruit ripening and aroma biogenesis
-
-
-
additional information
?
-
-, Q8W2B3
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
-
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
-
additional information
?
-
-
in the pyruvamide-activated enzyme form, the flexible loop located on the beta-domain can transfer information to the active center thiamine diphosphate located at the interface of the alpha and gamma domains, overview
-
-
-
additional information
?
-
-
substrate specificity of the engineered KdcA mutant enzymes with branched and unbranched 2-oxo acid substrates, overview
-
-
-
additional information
?
-
-
thiamine-dependent decarboxylases/dehydrogenases can also carry out socalled carboligation reactions, where the central ThDP-bound enamine intermediate reacts with electrophilic substrates, YPDC can produce acetoin and acetolactate, resulting from the reaction of the central thiamine diphosphate-bound enamine with acetaldehyde and pyruvate, respectively, overview, analysis of the stereoselectivity for forming the carboligase products acetoin, acetolactate, and phenylacetylcarbinol by the YPDC mutants E477Q and D28A
-
-
-
additional information
?
-
-
does not act on phenylpyruvate
-
-
-
additional information
?
-
-
even with benzaldehyde as the only substrate no benzoin can be detected, the enzyme does not produce (S)-2-hydroxypropiophenone
-
-
-
additional information
?
-
-
PDC has no activity with benzoylformate
-
-
-
additional information
?
-
Cyberlindnera jadinii UNSW, Candida tropicalis LU57, Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
the enzyme also performs carboligation reactions
-
-
-
additional information
?
-
Zygosaccharomyces bisporus CBS 702
Q9UUT6
nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
P06672
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q8NK64, Q8NK65
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q12629
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
P06169
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q9UUT6
key enzyme in alcoholic fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
catalyzes the penultimate step in ethanol fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q93EN4
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
enzyme within the glycolytic pathway in fermenting cells
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
enzyme within the glycolytic pathway in fermenting cells
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q96536
ethanol fermentation pathway, involved in anaerobic metabolism
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q9FVE1, -
involved in the enhancement of ethanol production in berries, but not the limiting factor
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-, Q8L388
key enzyme for the oxidative metabolism of lactic acid
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
key role in the alcoholic fermentation process
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
penultimate step in the alcoholic fermentation process
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
penultimate step of alcohol fermentation
-
ir
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Q659I2, -
enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
A2XFI3, -
Pdc is involved in the operation of ethanolic fermentation pathway that appears to correlate to an extent with anoxia tolerance in plants, overview
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
-
regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Cyberlindnera jadinii UNSW
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Sarcina ventriculi Goodsir
Q93EN4
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Candida tropicalis LU57
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Kluyveromyces lactis JA-6
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Saccharomyces cerevisiae WS34/70
-
penultimate step in the alcoholic fermentation process
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
-
-
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Zygosaccharomyces bisporus CBS 702
Q9UUT6
key enzyme in alcoholic fermentation
-
?
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
Acetobacter pasteurianus NCIB8618
Q8L388
key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
Cyberlindnera jadinii UNSW
-
-
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
show the reaction diagram
Candida tropicalis LU57, Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
Cyberlindnera jadinii UNSW
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
Cyberlindnera jadinii UNSW, Candida tropicalis LU57, Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
a 2-oxo acid
an aldehyde + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
key enzyme in ethanol formation
-
-
-
additional information
?
-
-
key enzyme in ethanol formation
-
-
-
additional information
?
-
-
key enzyme in alcoholic fermentation
-
-
-
additional information
?
-
-
pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
-
-
-
additional information
?
-
-
key enzyme in glycolytic pathway to ethanol
-
-
-
additional information
?
-
-
involved in a pathway in which NAD+ is regenerated under anaerobic conditions
-
-
-
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
-
additional information
?
-
-
one of the key enzymes involved in fermentation process
-
-
-
additional information
?
-
-
critical enzyme in a pollen-specific pathway to bypass pyruvate dehydrogenase enzymes and maintain biosynthetic capacity and energy production under the unique conditions prevailing during pollen-pistil interaction
-
-
-
additional information
?
-
-
involved in aerobic fermentation in mature pollen
-
-
-
additional information
?
-
-, Q8W2B3
involved in fruit ripening and aroma biogenesis
-
-
-
additional information
?
-
-, Q8W2B3
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
-
additional information
?
-
Cyberlindnera jadinii, Saccharomyces cerevisiae, Candida tropicalis, Kluyveromyces marxianus, Cyberlindnera jadinii UNSW, Candida tropicalis LU57, Kluyveromyces marxianus UNSW 510700, Saccharomyces cerevisiae UNSW
-
the enzyme also performs carboligation reactions
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CoA
-
desulfocoenzyme A can substitute for CoA showing that the cofactor plays a structural rather than a catalytic role
thiamine diphosphate
-, Q8L388
-
thiamine diphosphate
-
mode of active site binding, contains 1 mol thiamine diphosphate per subunit
thiamine diphosphate
-
requirement, located at the active site at the interface of the alpha and gamma domains
thiamine diphosphate
-
cofactor activation
thiamine diphosphate
-
requirement, mode of active site binding
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
Q9UUT6
-
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
-
coenzyme, bound in the interface between two subunits, binds pH-dependently
thiamine diphosphate
-
requirement
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
thiamine diphosphate
-
prosthetic group
thiamine diphosphate
Q93EN4
bound with high affinity at slightly acidic pH
thiamine diphosphate
-, Q6FJA3
-
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
thiamine diphosphate
Q8NK64, Q8NK65
;
thiamine diphosphate
Q12629
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
P06169
dependent on, bound tightly, but not covalently, at the interface of two monomers
thiamine diphosphate
-
-
thiamine diphosphate
A2XFI3, -
-
thiamine diphosphate
Q659I2, -
-
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
dependent on
thiamine diphosphate
-
0.1 mM, required for activity
thiamine diphosphate
-
dependent on
thiamine diphosphate
-
-
thiamine diphosphate
-
1.5 mM, required for activity
thiamine diphosphate
-
-
thiamine diphosphate
-
essential cofactor
thiamine diphosphate
-
-
thiamine diphosphate
-
dependent on
thiamine diphosphate
-
dependent on
thiamine diphosphate
-
dependent on
thiamine diphosphate
B0ZS79, -
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
0.5 mM, metal ions activate in descending order: Mg2+, Zn2+, Mn2+, Ca2+
Mg2+
-
Km: 0.024 mM
Mg2+
-
0.5 mM, metal ions activate in the descending order: Mg2+, Zn2+, Mn2+, Ca2+
Mg2+
-
cofactor
Mg2+
-
cofactor
Mg2+
-, Q8L388
cofactor
Mg2+
-
cofactor, mode of active site binding, contains 1 mol Mg2+ per subunit
Mg2+
-
cofactor, activates
Mg2+
-
cofactor, requirement
Mg2+
Q9UUT6
cofactor
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+
-
cofactor, tetramer binds 4 Mg2+ ions, tightly bound at pH 6, dissociates reversibly above pH 7
Mg2+
-
cofactor, requirement
Mg2+
Q93EN4
cofactor, bound with high affinity at slightly acidic pH
Mg2+
-, Q6FJA3
required
Mg2+
-
required
Mg2+
-
required for activity
Mg2+
Q8NK64, Q8NK65
highly required; highly required
Mg2+
Q12629
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+
P06169
dependent on, bound tightly, but not covalently, at the interface of two monomers
Mg2+
A2XFI3, -
-
Mg2+
-
required for activity
Mg2+
-
required for activity
Zn2+
-
0.5 mM, metal ions activate in descending order: Mg2+, Zn2+, Mn2+, Ca2+
Mn2+
-
0.5 mM, metal ions activate in descending order: Mg2+, Zn2+, Mn2+, Ca2+
additional information
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
-
-
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
-
wild type enzyme and mutant enzymes D28A, H114F, H115F and E477Q
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
-
reversible
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphoryldifluoromethyl)phosphonic acid
-
-
([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]hydroxyphosphorylmethyl) phosphonic acid
-
-
1,10-phenanthroline
Q684J7
1 mM, 95% inhibition
2,6-dichlorophenolindophenol
-
0.1 mM, weak inhibition
2-Hydroxy-5-nitrobenzyl-dimethylsulfonium bromide
-
-
2-p-Toluidinonaphthalene-6-sulfonate
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethanol
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-5-methyl-1H-[1,2,3]triazol-4-yl]ethyl diphosphate
-
-
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
a thiamine diphosphate analogue, almost irreversible inhibition
2-[1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1H-1,2,3-triazol-4-yl]ethyl trihydrogen diphosphate
-
a methyl triazole analogue of thiamine diphosphate, almost irreversible inhibition
3-deazathiamine diphosphate
-
12-step synthesis of the isoelectronic thiophene analogue of thiamine diphosphate, overview
3-hydroxypyruvate
-
-
acetaldehyde
-
inhibits, more resistant than PDC from Zymomonas mobilis, 8 mM, 2h, stable
acetaldehyde
-
0.4 mM, inactivates
Ag+
-, Q6FJA3
complete inhibition at 20 mM
benzaldehyde
-
inhibits formation of (R)-1-phenyl-1-hydroxy-propane-2-one
benzaldehyde
-
after a 20 h incubation with 30 mM benzaldehyde, the residual activity is 84% of the initial activity, enzyme stability dramatically decreases in the presence of 200 mM benzaldehyde (27% residual activity after 3 h incubation)
Co2+
-
slight
Cu+
-, Q6FJA3
complete inhibition at 20 mM
Cu2+
Q684J7
1 mM, 95% inhibition
ethylendiaminetetraacetate
Q684J7
1 mM, 95% inhibition
glyoxalate
-
mechanism-based inhibitor
glyoxalate
-
-
glyoxalate
-
irreversible
glyoxylate
-, Q6FJA3
complete inhibition
glyoxylic acid
P06169
-
Guanidinium chloride
-
6 M, denaturates
Hg2+
-
0.15 mM, 50% inhibition
iodoacetamide
-
-
KH2PO4
-
-
Lactate
-
-
maleate buffer
Q93EN4
inhibits at low pyruvate concentrations
-
Mn2+
-
slight
mono(2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl) iminodiacetate
-
-
N-([2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethoxy]sulfonyl)phosphoramidic acid
-
-
Ni2+
-
slight
O-2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl sulfamate
-
-
Omeprazole
-
50% inhibition at 0.016 mg/ml for enzyme from metronidazole-resistant strain or from cells grown under iron-limited conditions, little effect on enzyme from metronidazole-susceptible strain
p-chloromercuribenzoate
-
reversed by dithiothreitol
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
Q684J7
1 mM, 40% inhibition
phenylpyruvate
Q9UUT6
10 mM, 81% inhibition
phosphate
-
poor inhibitor at high concentrations
phosphate
-
-
phosphate
-
; competitive inhibition
phosphoramidon
Q684J7
1 mM, 48% inhibition
Pyruvamide
-
inhibits at high concentrations
Pyruvamide
-
mixed type inhibitor
pyruvate
-
substrate inhibition at high concentrations
pyruvate
-
modest substrate inhibition at high concentrations
pyruvate
Q9UUT6
substrate inhibition above 25 mM
pyruvate
-
weak substrate inhibition, above 100 mM
pyruvate
Q8NK64, Q8NK65
substrate inhibition at pyruvate concentrations above 20 mM for isoenzyme 1; substrate inhibition at pyruvate concentrations above 40 mM for isoenzyme 2
Sr2+
-
slight
thiamine diphosphate
-, Q6FJA3
PDC I, complete inhibition at 75 mM, PDC II, complete inhibition at 100 mM
Urea
-
8 M, denaturates
Zn2+
-
0.5 mM ZnCl2, 82% reduction of activity
Zn2+
-
slight
Zn2+
Q684J7
1 mM, 35% inhibition
[(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
mono[2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl] malonate
-
-
additional information
-
no product inhibition by (R)-1-phenyl-1-hydroxy-propane-2-one
-
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
Q93EN4
not inhibited by 25 mM EGTA or EDTA, at 37C, pH 6.5, 90 min, without cofactors
-
additional information
-
no inhibition by ferredoxin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
Ketomalonate
-
activates
NaCl
Q684J7
up to 3fold increase in activity at pH 5.4
phosphatidylcholine
-
activates at 2 mg/ml
Pyruvamide
-
activates
Pyruvamide
-
artificial activator
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
-
artificial activator
Pyruvamide
-
a substrate activator surrogate, activates, a flexible loop spanning residues 290 to 304 on the beta-domain of the enzyme, not seen in the absence of pyruvamide, occurs in presence of the activator, residues on the loop affect the enzyme activity, conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure
Pyruvamide
Q12629
the activator pyruvamide arrests the flexible loops comprising residues 106-113 and 292-301, so that two of four active sites become closed
Pyruvamide
P06169
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
-
substrate activation pathway from C221 to H92 to E91 to W412 to G413 to thiamine diphosphate, role of W412
pyruvate
-
substrate activation pathway, the consequences of binding substrate at C221 are propagated to the active site via the pathway H92 to E91 to W412 to G413 to thiamine diphosphate, role of C221 and E91
pyruvate
-
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, activation mechanism
pyruvate
-
allosteric substrate activation, alternating sites mechanism, random binding of pyruvate in the regulatory and active site, regulatory pyruvate is first bound to C-221 on the beta domain, binding generates a signal which is transmitted to the thiamine diphosphate cofactor, signal pathway, study of the pH-dependence of activation, two-step phenomenological model of activation, kinetics, pyruvate and pyruvamide have different activation pathways with distinct binding sites
pyruvate
-
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
Q9UUT6
substrate activation
pyruvate
-
substrate activation, mechanism
pyruvate
-
allosteric substrate activation, kinetics of dimeric and tetrameric enzyme
pyruvate
-
concentration-dependent substrate activation, minimum at 1.5 mM, mechanism, kinetics
pyruvate
Q93EN4
substrate activator is allosterically bound to enzyme, mechanism
pyruvate
-, Q6FJA3
-
pyruvate
Q12629
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
P06169
allosteric substrate activation, binding of substrate at a regulatory site induces catalytic activity, accompanied by conformational changes and subunit rearrangements
sodium bis(2-ethyl-1-hexyl)sulfosuccinate
-
a synthetic surfactant
Met32 protein
-
dependent upon Met32 protein
-
additional information
-, Q8L388
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
-
not activated by the substrate pyruvate
-
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
-
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
-
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
A2XFI3, -
induction of pdc1 is possibly a longterm response and pdc2 a short term response
-
additional information
Q659I2, -
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
-
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
-
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
-
additional information
-
enhanced PDC activity is observed in the skin tissue of fruit at early maturity stages
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.7
-
2-keto-4-methylhexanoic acid
-
mutant I472A, pH 6.5, 30C
3.7
-
2-keto-4-methylhexanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
40
-
2-keto-4-methylhexanoic acid
-
and above, wild type, pH 6.5, 30C
4.7
-
2-ketobutanoic acid
-
wild type, pH 6.5, 30C
6.7
-
2-ketobutanoic acid
-
mutant I472A, pH 6.5, 30C
50
-
2-ketobutanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
2.86
-
2-Ketobutyrate
-
30C, wild-type PDC
2.2
-
2-Ketobutyric acid
-
in 100 mM MES buffer (pH 5.6), 5 mM MgCl2, 1 mM dithiothreitol, and 1 mM thiamine diphosphate, at 25C
0.2
-
2-ketohexanoic acid
-
mutant I472A, pH 6.5, 30C
0.5
-
2-ketohexanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
12.7
-
2-ketohexanoic acid
-
wild type, pH 6.5, 30C
2.5
-
2-ketopentanoic acid
-
mutant I472A, pH 6.5, 30C
7.6
-
2-ketopentanoic acid
-
wild type, pH 6.5, 30C
11
-
2-ketopentanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
12.9
-
2-Ketovalerate
-
30C, wild-type PDC
1.27
-
2-oxoisopentanoate
-
-
1.9
-
2-oxoisovalerate
Q684J7
pH 6.5, 37C
1.8
-
benzoylformate
-
mutant I472A, pH 6.5, 30C
0.042
-
pyruvate
-
in 100 mM MES buffer (pH 5.6), 5 mM MgCl2, 1 mM dithiothreitol, and 1 mM thiamine diphosphate, at 25C
0.117
-
pyruvate
-
-
0.15
-
pyruvate
-
mutant enzyme E473D, at 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.18
0.2
pyruvate
-
30C, E473D mutant PDC
0.24
-
pyruvate
-
pH 6, 30C
0.25
-
pyruvate
-
30C, D27E mutant PDC
0.3
-
pyruvate
-
-
0.31
-
pyruvate
-
wild type enzyme, at 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.38
-
pyruvate
-
-
0.4
-
pyruvate
-
pH 6.0
0.4
-
pyruvate
-
mutant enzyme E473Q, at 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.43
0.48
pyruvate
-
30C, D27N mutant PDC
0.5
-
pyruvate
-
mutant enzyme E50D
0.52
-
pyruvate
-
wild type enzyme and mutant enzyme E449D
0.55
-
pyruvate
-
histidine buffer, enzyme from healthy tissue
0.6
-
pyruvate
-
-
0.62
-
pyruvate
-
pH 6.2, 25C
0.66
0.68
pyruvate
-
30C, wild-type PDC
0.68
-
pyruvate
-
30C, wild-type PDC
0.71
-
pyruvate
-
mutant enzyme H114Q
0.75
-
pyruvate
-
-
0.8
-
pyruvate
-, Q6FJA3
isoform PDC I, pH 6.0, 30C
0.8
-
pyruvate
-
-
0.85
-
pyruvate
-
histidine buffer, enzyme from diseased tissue
0.86
-
pyruvate
-
mutant enzyme W487L
0.9
-
pyruvate
-, Q6FJA3
isoform PDC II, pH 6.0, 30C
0.95
-
pyruvate
-
mutant enzyme D440E and mutant enzyme N467D
0.97
-
pyruvate
-
mutant enzyme F496I
1.04
1.17
pyruvate
-
30C, E473Q mutant PDC
1.06
-
pyruvate
-
mutant enzyme F496H
1.1
-
pyruvate
-
wild type, pH 6.5, 30C
1.1
-
pyruvate
-
pH and temperature not specified in the publication
1.25
-
pyruvate
-
pH 6.2, 25C, presence of 0.1 M NaCl
1.33
-
pyruvate
-
mutant enzyme V111A
1.7
-
pyruvate
-
phosphate buffer, enzyme from healthy tissue
1.73
-
pyruvate
Q9UUT6
pH 6, 25C, sigmoidal dependence of the reaction rate from substrate concentration, Hill coefficient 2.10
2.3
-
pyruvate
-
phosphate buffer, enzyme from diseased tissue
2.5
-
pyruvate
-
in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
2.6
-
pyruvate
-
mutant I476F, pH 6.5, 30C
2.8
-
pyruvate
Q93EN4
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
-
pyruvate
-
-
3.9
-
pyruvate
Q8NK64, Q8NK65
pH 6.5, 35C, isozyme 1
4.4
-
pyruvate
-
-
4.5
-
pyruvate
Q8NK64, Q8NK65
pH 6.5, 35C, isozyme 2
7.8
-
pyruvate
-
mutant I472A, pH 6.5, 30C
10
-
pyruvate
Q93EN4
pH 6.5, sodium hydrogen maleate buffer, two affinities for pyruvate, sigmoidal kinetics
50
-
pyruvate
-
mutant I472A/I476F, pH 6.5, 30C
18
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant V461I
22
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant M538W
34
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant S286Y
65
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant F381W
4.4
-
benzoylformate
-
mutant I472A/I476F, pH 6.5, 30C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data
-
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, pH-dependence of steady-state kinetic parameters
-
additional information
-
additional information
-
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle
-
additional information
-
additional information
-
kinetic data
-
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
-
additional information
-
additional information
-
kinetic data, kinetic model
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic studies
-
additional information
-
additional information
-
pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview
-
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
Q8NK64, Q8NK65
the isozyme shows sigmoidal kinetics with a Hill coefficient of 1.8; the isozyme shows sigmoidal kinetics with a Hill coefficient of 1.8
-
additional information
-
additional information
-
binding affinity of CoA is 0.11 mM
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
2-keto-4-methylhexanoic acid
-
wild type, pH 6.5, 30C
7.7
-
2-keto-4-methylhexanoic acid
-
mutant I472A, pH 6.5, 30C
8.1
-
2-keto-4-methylhexanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
9
-
2-ketobutanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
32
-
2-ketobutanoic acid
-
mutant I476F, pH 6.5, 30C
250
-
2-ketobutanoic acid
-
mutant I472A, pH 6.5, 30C
320
-
2-ketobutanoic acid
-
wild type, pH 6.5, 30C
9
-
2-Ketobutyrate
-
30C, wild-type PDC
61.4
-
2-Ketobutyrate
-
30C, wild-type PDC
0.8
-
2-ketohexanoic acid
-
mutant I476F, pH 6.5, 30C
4
-
2-ketohexanoic acid
-
wild type, pH 6.5, 30C
82
-
2-ketohexanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
130
-
2-ketohexanoic acid
-
mutant I472A, pH 6.5, 30C
11
-
2-ketopentanoic acid
-
mutant I476F, pH 6.5, 30C
30
-
2-ketopentanoic acid
-
mutant I472A/I476F, pH 6.5, 30C
53
-
2-ketopentanoic acid
-
wild type, pH 6.5, 30C
220
-
2-ketopentanoic acid
-
mutant I472A, pH 6.5, 30C
13.7
-
2-Ketovalerate
-
30C, wild-type PDC
1.2
-
benzoylformate
-
mutant I472A/I476F, pH 6.5, 30C
0.03
0.55
pyruvate
-
pH 6, 25C, W412A mutant PDC
0.1
-
pyruvate
-
mutant enzyme E473D, at 30C 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 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.99
-
pyruvate
-
pH 6, 25C, C221E/C222A double mutant YPDC
2.1
-
pyruvate
-
pH 6, 25C, wild-type PDC
2.5
-
pyruvate
-
pH 6, 4C, C221A/C222A double mutant PDC
3.1
-
pyruvate
-
pH 6, 25C, E91A mutant PDC
3.8
-
pyruvate
-
pH 6, 25C, C221D/C222A double mutant YPDC
6.55
-
pyruvate
-
pH 6, 25C, W412A mutant PDC
8
-
pyruvate
-
mutant I472A/I476F, pH 6.5, 30C
10
-
pyruvate
-
pH 6, 4C, wild-type PDC
15
-
pyruvate
-
pH 6, 30C, C221A/C222A double mutant PDC
17.5
-
pyruvate
-
pH 6, 25C, E91D mutant PDC
17.8
-
pyruvate
-
pH 6, 25C, W412F mutant PDC
20.4
-
pyruvate
-
pH 6, 25C, E91Q mutant PDC
40
-
pyruvate
-
pH 6, 30C, enzyme monomer
43.6
-
pyruvate
-, Q6FJA3
isoform PDC I, pH 6.0, 30C
73.1
-
pyruvate
-
pH 6, 25C, wild-type PDC
77
-
pyruvate
-, Q6FJA3
isoform PDC II, pH 6.0, 30C
77
-
pyruvate
-
mutant I476F, pH 6.5, 30C
113
-
pyruvate
-
30C, wild-type PDC
120
-
pyruvate
-
-
150
-
pyruvate
-
wild type enzyme, at 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
200
-
pyruvate
-
mutant I472A, pH 6.5, 30C
486
-
pyruvate
-
wild type, pH 6.5, 30C
2.3
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant V461I
2.5
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant M538W
17
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant S286Y
26
-
Pyruvic acid
-
pH 6.0, 30C, recombinant mutant F381W
6.9
-
benzoylformate
-
mutant I472A, pH 6.5, 30C
additional information
-
additional information
-
kcat values at different pH values from pH 4.5 to 7.5 of wild-type, W412F and W412A mutant PDC
-
additional information
-
additional information
-
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/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.38
-
pyruvate
-
mutant enzyme E473Q, at 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
16065
0.67
-
pyruvate
-
mutant enzyme E473D, at 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
16065
484
-
pyruvate
-
wild type enzyme, at 30C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
16065
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
0.000000014
-
3-deazathiamine diphosphate
-
below
0.15
-
Hg2+
-
-
0.4
-
mono(2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl) iminodiacetate
-
-
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
-
-
14.7
-
phosphate
-
native enzyme, at pH 6.0 and 30C; wild type enzyme, at pH 6.0 and 30C
51
-
phosphate
-
mutant enzyme A143T/T156A/Q367H/N396I/K478R, at pH 6.0 and 30C
1.45
-
pyruvate
-
pH 6, D28N mutant YPDC
3.04
-
pyruvate
-
pH 6, D28A mutant YPDC
3.75
-
pyruvate
-
D28A mutant YPDC
112.2
-
pyruvate
-
pH 6, E477Q mutant YPDC
136
-
pyruvate
-
pH 6, E477Q mutant YPDC
433
-
pyruvate
-
pH 6, wild-type YPDC
1200
-
pyruvate
-
pH 6, 30C
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
-
-
0.4
-
mono[2-[1-(4-amino-2-methylpyrimidin-5-ylmethyl)-1H-[1,2,3]triazol-4-yl]ethyl] malonate
-
-
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.02
0.03
-
pH 6, 20C, D28A mutant YPDC
0.04
0.07
-
pH 6, 20C, D28N mutant YPDC
0.1
0.15
-
pH 6, 20C, E477Q mutant YPDC
0.1
-
-
crude extract, at 25C
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
0.29
-
-
30C, growth on ethanol, aerobic conditions
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; using 3-fluoro-2-oxopropanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
-
using 4-methyl-2-oxopentanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
0.3
-
-
using 2-oxo-4-phenylbutanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate; 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
0.4
-
-
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
-
-
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; 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
0.64
-
-
30C, growth on galactose, aerobic conditions
0.8
-
-
using phenylpyruvate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
0.95
-
-
30C, growth on glucose, aerobic conditions
1.1
-
-
using 11 as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate; using 2-oxooctanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate; 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
1.7
-
-
using 2-oxo-4-phenylbutanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
1.8
-
-
using phenylpyruvate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
1.81
-
-
30C, growth on glucose, anaerobic conditions
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
-
-
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; 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
3.71
-
-
diseased preparations
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
5.3
-
-
using 2-oxohexanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
5.7
-
-
pH 6.2, 25C, metronidazole-resistant strain
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
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
-
-
-
12.3
-
-
healthy preparations
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
14.34
-
-
after 143fold purification, at 25C
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
20.7
-
-
using 2-oxopentanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
21.7
-
-, Q6FJA3
isoform PDC I, pH 6.0, 30C
40
45
-
pH 6, 20C, wild-type YPDC
40
-
-, Q6FJA3
isoform PDC II, pH 6.0, 30C
41.6
-
-
roots
43
46
-
pH 6, 30C
43.4
-
-
using pyruvate as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
45
50
-
pH 6, 25C, wild-type PDC
59.4
-
Q8NK64, Q8NK65
purified native isozymes
60
-
-
using 2-oxobutanoic acid as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
75.4
-
Q8NK64, Q8NK65
purified native isozyme
80.7
-
Q684J7
pH 6.5, 37C
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
96.4
-
-
kernel
147
-
-
using pyruvate as substrate, in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
515
-
-
pH 6, 25C, C221A/C222A double mutant PDC
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-, Q8L388
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
carboligase reaction, wild-type and mutant YPDC, at different pH values
additional information
-
-
-
additional information
-
Q9UUT6
-
additional information
-
-
-
additional information
-
-
no difference in specific activity of dimeric and tetrameric enzyme state
additional information
-
-
-
additional information
-
-
activity in cell extracts grown on different media estimated with and without exogenous thiamine diphosphate
additional information
-
-
colorimetric assay based on formation of (R)-phenylacetylcarbinol
additional information
-
-
(R)-phenylacetylcarbinol production rate
additional information
-
A2XFI3, -
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.3
-
-
2 pH-optima: a major peak at pH 6.0 and a minor peak at pH 4.3
5.5
-
-
for decarboxylation
5.7
6.3
Q12629
-
5.7
6.3
P06169
-
5.8
6
-
wild-type YPDC
5.8
-
-
-
6
6.5
-, Q6FJA3
-
6
-
-
2 pH-optima: a major peak at pH 6.0 and a minor peak at pH 4.3
6
-
-
-
6
-
Q9UUT6
assay at
6
-
-, Q96536
assay at
6
-
-
assay at
6.1
6.6
-
-
6.3
6.5
Q8NK64, Q8NK65
;
6.3
-
-
-
6.5
7
-
carboligation of acetaldehyde and benzaldehyde, optimal activity in potassium phosphate buffer
6.5
-
-
assay at
6.5
-
Q684J7
-
6.5
-
-
assay at
6.5
-
-
assay at
6.5
-
-
for carboligation
6.6
-
-
wild-type enzyme
6.8
-
-
dimer and tetramer
7.5
-
-
decarboxylation of hydroxypyruvate, negligible activity with pyruvate
additional information
-
-
-
additional information
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
8
-
pH 4.6: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
5
-
-
about 50% of maximal activity at pH 5.0 and at pH 7.5
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
5.5
7.5
Q684J7
-
5.9
8
Q8NK64, Q8NK65
16% of maximal activity at pH 8.0; 16% of maximal activity at pH 8.0
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
-
-
-
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
21
-
-
assay at
25
-
Q9UUT6
assay at
25
-
-, Q96536
assay at
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
native Pdc1 performs optimally at 30C in 1 mM pyruvate; the optimal temperature for Pdc1 activity is dependent upon pyruvate concentration, in 1 mM pyruvate, native Pdc1 performs optimally at 30C
35
-
Q8NK64, Q8NK65
assay at; assay at
45
-
Q684J7
-
45
-
-
native activity peaks at 45C in 25 mM pyruvate; the optimal temperature for Pdc1 activity is dependent upon pyruvate concentration, in 25 mM pyruvate, native activity peaks at 45?C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
30
-
enzyme is 6times more active at 30C than at 4C
20
30
-
only slightly differing catalytic activity in the range, +/-10% relative to 25C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
-
Q93EN4
calculated from the sequence
5.49
-
-, Q8L388
calculated from the amino acid sequence
5.82
-
Q8NK64, Q8NK65
isozyme 2, 2D electrophoresis
5.94
-
Q8NK64, Q8NK65
isozyme 1, 2D electrophoresis
6.45
-
-, Q8W2B3
calculated
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Kluyveromyces lactis JA-6
-
-
-
Manually annotated by BRENDA team
Q93EN4
recombinant PDC, expressed in Escherichia coli
-
Manually annotated by BRENDA team
Sarcina ventriculi Goodsir
-
recombinant PDC, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60000
-
-
SDS-PAGE
60800
-
-
gel filtration
65000
-
-
SDS-PAGE
120000
128000
Q8NK64, Q8NK65
dimeric enzyme form, native PAGE; dimeric enzyme form, native PAGE
120000
-
-, Q6FJA3
PAGE
150000
-
-, Q6FJA3
gel filtration
200000
-
-
gel filtration
200000
-
-
about, wild-type PDC, gel filtration
200000
-
-
about, gel filtration
209000
-
-
gel filtration
210000
-
-
gel filtration
219700
-
-
gel filtration
220000
240000
-
gel filtration
235000
-
Q93EN4
recombinant PDC, pH 6.5, gel filtration
240000
-
-
gel filtration
240000
-
-
disc gel electrophoresis
240000
-
-
native PAGE
240000
-
-
gel filtration
240000
-
-
wild-type and E473Q mutant PDC, gel filtration
240000
-
-
native tetrameric PDC
240000
-
-
tetramer
240000
-
-
gel filtration
240000
-
-
gel filtration
240000
-
Q684J7
gel filtration
240000
-
Q12629
-
240000
-
P06169
-
244000
-
Q9UUT6
active enzyme, gel filtration
272000
-
Q8NK64, Q8NK65
tetrameric enzyme form, native PAGE; tetrameric enzyme form, native PAGE
390000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
2 protein bands detected in SDS-PAGE: 65000 and 68000, the enzyme exists as a mixture of tetramers, octamers and higher oligomers
?
-
2 types of subunits, MW 61000 and MW 62000, SDS-PAGE
?
-, Q8L388
x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
?
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
?
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
?
-
x * 63000, SDS-PAGE
?
-, Q8W2B3
x * 65300, calculated
?
-
x * 58000, recombinant enzyme, SDS-PAGE
?
A2XFI3, -
x * 64000, alpha-subunit + x * 62000, beta-subunit
?
Acetobacter pasteurianus NCIB8618
-
x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
-
dimer
-
1 * 39800 + 1 * 41700, the dimeric pyruvate decarboxylase is a component of the multienzyme complex pyruvate dehydrogenase, SDS-PAGE
dimer
-
catalytically active form
dimer
-, Q6FJA3
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
dimer
Q8NK64, Q8NK65
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form; 2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
dimer
Candida glabrata IFO005
-
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
-
heterotetramer
-
native, catalytically active form, dimer of dimers
homodimer
-
2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
homotetramer
-
4 * 60800, wild-type PDC, SDS-PAGE
homotetramer
-
-
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
Q9UUT6
alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
homotetramer
-
4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
homotetramer
Q93EN4
4 * 58000, recombinant PDC, pH 6.5, SDS-PAGE
homotetramer
Sarcina ventriculi Goodsir
-
4 * 58000, recombinant PDC, pH 6.5, SDS-PAGE
-
homotetramer
Zygosaccharomyces bisporus CBS 702
-
alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
-
monomer
-
1 * 60000, alpha subunit, catalytically inactive form
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
4 * 56500, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 62000-64000, SDS-PAGE
tetramer
-
two of the dimers form a tightly packed tetramer with pseudo 222 symmetry
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 59000, SDS-PAGE; 4 * 60746, SDS-PAGE
tetramer
-
4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE
tetramer
-
enzyme structure, differences in the tetramer assembly of form A and B PDC, form A is the native PDC
tetramer
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
Q684J7
4 * 61000, calculated, 4 * 66000, SDS-PAGE
tetramer
Q8NK64, Q8NK65
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form; 2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
tetramer
Q12629
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
P06169
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
Kluyveromyces lactis JA-6
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
-
tetramer
Saccharomyces cerevisiae WS34/70
-
enzyme structure, differences in the tetramer assembly of form A and B PDC, form A is the native PDC
-
monomer
-
1 * 60000, catalytically inactive enzyme state, SDS-PAGE
additional information
-
two types of protein chains detected by SDS-PAGE: MW 63000-65000 and MW 61000-62000
additional information
-
one isoenzyme has the subunit structure alpha4 and the other has the subunit structure alpha2'beta2
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
-
hydroxyl-ion-induced subunit dissociation
additional information
-
thiamine diphosphate is required for complete association of subunits to form active oligomer
additional information
-
phosphate stabilizes the tetramer by shifting the dimer-tetramer equilibrium to higher pH values, without altering the conformation of the tetramer
additional information
-
4 * 62000, SDS-PAGE
additional information
-
different oligomeric states, tetramers, dimers and monomers, of enzyme occur under defined conditions, unfolding kinetics, tetramers dissociate via a stable dimeric state into monomers
additional information
-
treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
additional information
-
conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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, 8C, 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
Q12629
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
A2XFI3, -
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)
P06169
PDC complex with pyruvamide
-
X-ray crystallography structure
-
crystal structure
-
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))
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9
-
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
-
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
-
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
-
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
6
-
-
maximal stability
6.5
7.5
-, Q6FJA3
-
8
-
-
above pH 8 the enzyme dissociates into two dimeric subunits
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
95
-
thermal denaturation study
20
35
-
half-life of 235 h at 20C, half-life of 78 h at 30C, half-life of 62 h at 35C
25
-
-
rapidly inactivated at
30
60
-
half-life of 150 h at 30C, 40 h at 40C, 10 h at 50C, and 0.4 h at 60C
30
70
-
half-life of 144 h at 30C, 34 h at 40C, 12 h at 50C, 2 h at 60C, and 0.4 h at 70C
30
-
-
rapidly inactivated at
38
-
-
rapid inactivation above
38.5
-
-
Tm, E91A mutant PDC
40
-
-
Tm, W412A mutant PDC
40
-
-, Q6FJA3
1 h, 73.2% residual activity, isoform PDC, 93.2% residual activity, isoform PDC II
42
-
Q93EN4
in presence of 1 mM thiamine diphosphate, 1 mM Mg2+, pH 6.5, stable up to
42.5
-
-
Tm, E91D mutant PDC
45
65
-
the activity of native Pdc1 decreases with increasing temperature from 45C and is completely abolished at 65C, the temperature at which half of the native Pdc1 activity is irreversibly lost in 5 min is at 52.6C
45
-
Q684J7
30 min, complete inactivation
45.5
-
-
Tm, E91Q mutant PDC
50
-
Q93EN4
60-90 min, complete loss of activity
50
-
-, Q6FJA3
1 h, 23.9% residual activity, isoform PDC, 43.1% residual activity, isoform PDC II
51.5
-
-
Tm, W412F mutant PDC
52.6
-
-
50% activity is lost after 5 min at 52.6C
59.5
-
-
Tm, wild-type PDC
60
-
-, Q6FJA3
1 h, 3% residual activity, isoform PDC, 2.7% residual activity, isoform PDC II
65
-
-
30 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0.1 mM thiamine diphosphate is sufficient to keep the enzyme stable and active in potassium phosphate buffer for several days
-
6C, 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
-
half-life of 7 days for both crude enzyme extract and whole cell biomass preparations in presence of 50 mM benzaldehyde at 22C, half-life of nearly 2 weeks for crude enzyme extract and slightly longer for whole cell biomass in absence of benzaldehyde
-
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 22C
-
Mg2+ and thiamin diphosphate stabilize
-
not sensitive to low ionic strength, 10 mM buffer
-
not stabilized by addition of ammonium sulfate
-
0.1 mM thiamine diphosphate is sufficient to keep the enzyme stable and active in potassium phosphate buffer for several days
-
central role of the beta domain in stabilizing the overall structure
-
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 22C
-
low stability in the isolated state, less stable than PDC from Zymomonas mobilis
-
native Pdc1 activity is not altered by a His-tag
-
the enzyme in phosphate buffer pressurized with CO2 up to 9 MPa for 1 h at 35C 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
-
thiamine diphosphate and Mg2+ stabilize
-
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
-
stability with respect to purification degree
-
0.1 mM thiamine diphosphate is sufficient to keep the enzyme stable and active in potassium phosphate buffer for several days
-
more stable than PDC from Saccharomyces cerevisiae, stirring deactivates significantly
-
retains about 50% of activity in buffer supplemented with 2 M NaCl or KCl, retain 20% of activity in 4 M salt buffer
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
45 mM has no effect
urea
-
treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, lyophilized preparation, stable for at least 3 months
-, Q6FJA3
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 22C
-
-20C, little or no loss of activity after several months
-
-20C or -80C, pH 6.0, 1 mM thiamine diphosphate, 1 mM MgSO4, minimum protein concentration 0.2 mg/ml, stable for several months
-
-70C, 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
-
4C, wild-type and W412F mutant PDC, several months, stable
-
-20C, 50% ethylene glycol, stable for 3 months
-
-20C, concentrated PDC, buffered solution containing thiamine diphosphate and MgSO4, several months, stable
Q9UUT6
-20C, 50% v/v glycerol, negligible loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme partially
-
partial purification by acetone precipitation
-
native enzyme by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography to over 95% homogeneity
Q12629
recombinant enzyme mutants from Escherichia coli strain BL21(DE3)
-
partially purified, ammonium sulfate precipitation and phenyl Sepharose column chromatography
-
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
Q8NK64, Q8NK65
2 isoenzymes: I and II
-
HiTrap chelating column chromatography; HiTrap Ni2+ chelating HP column chromatography
-
native enzyme by acetone precipitation, ammonium sulfate fractionation, and gel filtration to over 95% homogeneity
P06169
recombinant homomeric, alpha-only, PDC1
-
recombinant mutants D28A and His6-tagged E477Q, the latter on a talon resin
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
W412F and W412A mutant PDC, expressed in Escherichia coli, W412A is purified as apoenzyme
-
wild-type and D28A, D28N, E477Q mutant YPDC
-
wild-type PDC and C221A/C222A double mutant
-
wild-type, C221E/C222A and C221A/C222A double mutant YPDC
-
wild-type, E91A, E91D and E91Q mutant PDC, expressed in Escherichia coli, mutants are purified as apoenzymes
-
136fold, recombinant PDC, expressed in Escherichia coli
Q93EN4
5 C-terminal deletion mutants
-
Fractogel EMD TMAE column chromatography and Superdex 200 gel filtration
-
PDC mutants D27E, D27N, E473D and E473Q
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression of pdc gene in recombinant Escherichia coli, sequencing, pdc operon
-, Q8L388
PDC2 gene, overexpression improves the tolerance of hairy roots to low oxygen conditions
-, Q96536
expressed in Hansenula polymorpha; expressed in Hansenula polymorpha strain NCYC495 leu1-1
-
recombinant expression
Q12629
expression of enzyme mutants in Escherichia coli strain BL21(DE3)
-
expressed in leaves of the Nicotiana tabacum transgenic line 9204-X
-
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
A2XFI3, -
expressed in Escherichia coli BL21(DE3)RecA- cells; expressed in Escherichia coli strain BL21(DE3)RecA-
-
expression in Escherichia coli BL21(DE3)
-
expression of mutants D28A and His6-tagged E477Q
-
expression of W412F and W412A mutant PDC in Escherichia coli BL21(DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of wild-type, E91A, E91D and E91Q mutant PDC in Escherichia coli BL21(DE3)
-
overexpression of wild-type and mutant YPDC in Escherichia coli BL21
-
recombinant expression
P06169
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
-
pdc gene, sequencing, expression in Escherichia coli BL-21-CodonPlus-RIL containing plasmid pSJS1240
Q93EN4
2 pyruvate decarboxylase genes diverge significantly from one another and from other yeast pyruvate decarboxylase genes
-
nucleotide sequence
Q9FVE1, -
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
Q659I2, -
cDNA sequence
Q9UUT6
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Geobacillus thermoglucosidasius
-
expressed in Escherichia coli strain BL21
-
expressed in Escherichia coli strain KO11
-
expressed in Escherichia coli strains CCE14 and KO11
-
expressed in Geobacillus thermoglucosidasius; expressed in Geobacillus thermoglucosidasius strain TN
-
expressed in Hansenula polymorpha
-
expressed in the ethanol-tolerant Escherichia coli mutant ET1bc
-
expression in Escherichia coli
-
expression of PDC mutants D27E, D27N, E473D and E473Q in Escherichia coli
-
expression of wild-type and W392M mutant PDC in Escherichia coli K12
-
expression of wild-type PDC and C-terminal deletion mutants in Escherichia coli
-
wild type enzyme is expressed in Escherichia coli SG13009 cells, mutant enzymes E473D and E473Q are expressed in Escherichia coli JM109 cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
for PDC, the level of transcripts remain quantitatively constant in all fruit maturity stages
B0ZS79, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D28A
-
the mutant is almost catalytically inactive
F381W
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme
M538W
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing higher kcat and activity with pyruvate compared to the wild-type enzyme
S286Y
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme
A143T/T156A/Q367H/N396I/K478R
-
mutant shows improved activity for 1 mM pyruvate at pH 7.5 in the presence of phosphate, has the substrate concentration required for half-saturation reduced by almost 3fold at pH 7.5 and the phosphate inhibition reduced by 4fold at pH 6.0 compared to the wild type enzyme, the mutant can be activated by pyruvate more easily than the native enzyme; 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
-
mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6
C221A
-
active mutant with reduced Hill coefficient of 1
C221A/C222A
-
active double mutant without substrate activation, effect of modified substrate-activation site on catalysis, kinetic properties
C221A/C222A
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active double mutant, effect on transition states
C221D
-
mutant with nearly wild-type activity, hyperbolic kinetics
C221D/C222A
-
double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics
C221E
-
mutant with nearly wild-type activity, hyperbolic kinetics
C221E/C222A
-
double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics
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
-
mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6
C221S
-
active mutant with reduced Hill coefficient of 0.8-0.9
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
-
inactivated faster than the wild type enzyme
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
-
active site mutant with very low activity
D28A
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
D28A
P06169
the mutant is almost catalytically inactive
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
-
active site mutant with very low activity
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
-
inactivated faster than 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
-
active site mutant with very low activity
E477Q
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
E477Q
P06169
the mutant is almost catalytically inactive
E477Q/E91D
-
retains catalytic activity
E51D
-
mutant with 50% of wild-type acetaldehyde producing activity
E51D/E91D
-
no residual catalytic activity
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
-
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
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
-
inactivated faster than the wild type enzyme
H114F
-
active site mutant
H115F
-
inactivated faster than the wild type enzyme
H115F
-
active site mutant
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
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
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
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
-
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
E50D
-
2.9% of wild-type activity
E50Q
-
0.46% of wild-type activity
I472A/I476F
-
increase in substrate binding affinity and specificity, highest enantioselectivity for (S)-acetoin, very low yield of product
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
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
E477Q
-
the mutant is almost catalytically inactive
additional information
-
each of isoform genes PDC11, PDC12, PDC13, can complement Saccharomyces cerevisiae pdc null mutant strains
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
additional information
A2XFI3, -
production and phenotypic analysis of rice transgenics with altered levels of pyruvate decarboxylase protein, Pdc overexpressing rice transgenics at early seedling stage under unstressed control growth conditions showed slight, consistent advantage in root vigour as compared to that of wild-type seedlings, overview
additional information
-
enzyme null mutant, growth of mutant pollen tubes through the style is reduced, and the mutant allele shows reduced transmission through the male, when in competition with wild-type pollen
L111V
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site-directed mutagenesis, the mutant shows 21% of the wild-type kcat
additional information
-
construction of mutant pdc-803 with a S296DELTAF297DELTA deletion, the mutant shows highly reduced activity compared to the wild-type enzyme
W412F
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency
additional information
-
engineering of Lactobacillus brevis strain ATCC367 to express Sarcina ventriculi pyruvate decarboxylase and Lactobacillus brevis alcohol dehydrogenase genes in order to increase ethanol fermentation from biomass-derived residues, the engineered strain is termed bbc03, overview
I476F
-
rapid loss of cofactor thiamine diphosphate. Improvement of enantioselectivity for (S)-acetoin
additional information
-
engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
Candida tropicalis LU57
-
PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
-
synthesis
-
Candida utilis PDC is a stable and high productivity enzyme for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
Cyberlindnera jadinii UNSW
-
Candida utilis PDC is a stable and high productivity enzyme for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
-
synthesis
-
PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
Kluyveromyces marxianus UNSW 510700
-
PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
-
synthesis
-
engineered enzyme mutants are useful for synthesis of both enantiomers of alpha-ketols and acetolactates with good enantiomeric excess, overview
synthesis
-
PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
synthesis
Saccharomyces cerevisiae UNSW
-
PDC is useful for the production (R)-phenylacetylcarbinol, a pharmaceutical precursor
-
synthesis
-
the enzyme is useful in ethanol production in bacterial coupled systems, overview
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