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Information on EC 4.1.1.1 - pyruvate decarboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P06169
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4.1.1.1 pyruvate decarboxylaseIUBMB Comments
A thiamine-diphosphate protein. Also catalyses acyloin formation.
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Word Map
- 4.1.1.1
- dendritic
-
plasmacytoid
-
toll-like
- thiamin
-
claim
- autoimmune
-
prescript
- ifn-alpha
-
pharmacy
-
lymphoid
-
herbicide
- zymomonas
-
branched-chain
- cdc
- acetaldehyde
- mobilis
- sulfonylurea
-
real-world
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tregs
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adhes
- interferon-alpha
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insurance
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lupus
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antigen-presenting
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costimulatory
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lipoylated
- erythematosus
-
nonadherence
-
refill
-
medicare
-
tolerogenic
- dabigatran
- acetolactate
-
marketscan
-
dispensing
- synthesis
-
hla-dr
-
antimitochondrial
- acetoin
-
dihydrolipoyl
- biotechnology
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pharmacist
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herbicide-resistant
-
beneficiaries
-
icd-9-cm
- dihydrolipoamide
- transacetylase
- rivaroxaban
- dichloroacetate
-
enrollees
- lipoate
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
pdc, pyruvate decarboxylase, acetohydroxyacid synthase, yeast pyruvate decarboxylase, pdc1p, ifpl730, p59nc, pyruvate decarboxylase 1, zmpdc, pdc5p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PDC1
8-10 nm cytoplasmic filament-associated protein
-
-
-
-
alpha-Carboxylase
-
-
-
-
alpha-Keto acid carboxylase
-
-
-
-
Decarboxylase, pyruvate
-
-
-
-
P59NC
-
-
-
-
PDC
PDC1
Pdc1p
Pdc5
Pdc6
Pyruvic decarboxylase
-
-
-
-
YPDC
-
-
PDC
-
-
-
-
Pdc6
-
sulfur-poor pyruvate decarboxylase, third minor isozyme of pyruvate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 2-oxo carboxylate = an aldehyde + CO2
mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
catalytic mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
catalytic and kinetic mechanism, catalyzes carboligation as side reaction
-
a 2-oxo carboxylate = an aldehyde + CO2
catalytic mechanism, catalyzes the carboligation of 2 aldehydes as side reaction, mechanism
-
a 2-oxo carboxylate = an aldehyde + CO2
catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions
-
a 2-oxo carboxylate = an aldehyde + CO2
mechanism, catalyzes carboligation as side reaction
-
a 2-oxo carboxylate = an aldehyde + CO2
enzyme forms covalent intermediate C2-alpha-lactylthiamine diphosphate. Rate of reaction is limited by release of thiamine diphosphate
-
a 2-oxo carboxylate = an aldehyde + CO2
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
reaction mechanism, overview
-
a 2-oxo carboxylate = an aldehyde + CO2
mechanism of catalytic cycle of yeast pyruvate decarboxylase, overview. Pyruvate and analogues induce active site asymmetry in the wild-type yeast enzyme and mutant variants. The rare 1',4'-iminopyrimidine thiamine diphosphate tautomer participates in formation of thiamine diphosphate-bound intermediates. Propionylphosphinate also binds at the regulatory site and its binding is reflected by catalytic events at the active site 20 A away. The yeast enzyme stabilizes an electrostatic model for the 4'-aminopyrimidinium ionization state, an important contribution of the protein to catalysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-oxo-acid carboxy-lyase (aldehyde-forming)
A thiamine-diphosphate protein. Also catalyses acyloin formation.
CAS REGISTRY NUMBER
COMMENTARY
9001-04-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 pyruvate
(S)-acetolactate + CO2
-
D28A YPDC variant, not E477Q YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
3-Fluoropyruvate
acetate + F- + CO2
-
decarboxylation is followed by release of F-
-
?
acetaldehyde + acetaldehyde
acetoin
-
carboligation of 2 aldehydes as a side reaction of PDC
-
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
carboligation of 2 aldehydes as a side reaction of PDC, high carboligase activity, more active than PDC from Zymomonas mobilis
(R)-phenylacetylcarbinol
?
beta-hydroxypyruvate
2,4-dihydroxymethyl-3-oxo-butanoic acid
-
D28A YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
beta-hydroxypyruvate + glycolaldehyde
1,3,4-trihydroxy-2-butanone
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
4 active sites in the tetramer, enzyme structure
-
?
pyruvate
acetaldehyde + CO2
-
alternating sites mechanism
-
?
pyruvate
acetaldehyde + CO2
-
catalytic cycle, 3 domains: a diphosphate-binding domain, a pyrimidine-binding domain and a regulatory domain, model for enzyme regulation
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, acetaldehyde is produced by protonation of the key C2alpha-carbanion/enamine intermediate
-
ir
pyruvate
acetaldehyde + CO2
-
detailed mechanism with roles for the active center acid-base groups D28, E477, H114 and H115, catalytic cycle, mechanistic model of the reaction, alternating sites model
-
ir
pyruvate
acetaldehyde + CO2
-
detailed mechanism, catalytic cycle, alternating sites mechanism based on tight communication between active sites of the functional dimer, with the ionizable residues D28, E477 and H115 likely to be important in creating this communication, enzyme exists in three conformations, one inactive and two active forms, enzyme structure
-
ir
pyruvate
acetaldehyde + CO2
-
nonoxidative decarboxylation, main reaction
-
?
pyruvate
acetaldehyde + CO2
-
enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
key role in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step of alcohol fermentation
-
ir
pyruvate
acetaldehyde + CO2
-
regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
i.e. 3-hydroxy-2-butanone, formation of the (R)- and the (S)-enantiomers
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
the 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
?
-
-
oxidative diversion of the decarboxylation of pyruvate by 2,6-dichlorophenolindophenol, which traps a carbanionic intermediate and diverts the product from acetaldehyde to acetate, kinetics
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
in the pyruvamide-activated enzyme form, the flexible loop located on the beta-domain can transfer information to the active center thiamine diphosphate located at the interface of the alpha and gamma domains, overview
-
-
?
additional information
?
-
-
thiamine-dependent decarboxylases/dehydrogenases can also carry out socalled carboligation reactions, where the central ThDP-bound enamine intermediate reacts with electrophilic substrates, YPDC can produce acetoin and acetolactate, resulting from the reaction of the central thiamine diphosphate-bound enamine with acetaldehyde and pyruvate, respectively, overview, analysis of the stereoselectivity for forming the carboligase products acetoin, acetolactate, and phenylacetylcarbinol by the YPDC mutants E477Q and D28A
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
enzymatic stereoselective synthesis of L-norephedrine by coupling recombinant R-selective pyruvate decarboxylase from from Saccharomyces cerevisiae and an S-selective omega-transaminase from Vibrio fluvialis JS17, method optimization, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
key role in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step of alcohol fermentation
-
ir
pyruvate
acetaldehyde + CO2
-
regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
dependent on, bound tightly, but not covalently, at the interface of two monomers
thiamine diphosphate
-
-
thiamine diphosphate
-
coenzyme, bound in the interface between two subunits, binds pH-dependently
thiamine diphosphate
-
requirement, active center, at the interface of the alpha and gamma domains
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, located at the active site at the interface of the alpha and gamma domains
thiamine diphosphate
-
requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7
thiamine diphosphate
-
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
-
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
-
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps
thiamine diphosphate
-
required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
Mg2+
dependent on, bound tightly, but not covalently, at the interface of two monomers
Mg2+
-
cofactor, tetramer binds 4 Mg2+ ions, tightly bound at pH 6, dissociates reversibly above pH 7
Mg2+
-
essential for activity, coordinated in the active site at the diphosphate moiety of the coenzyme thiamine diphosphate, also able to coordinate to other specific functional groups than in the active site region, stabilizes the monomeric state of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetaldehyde
-
inhibits, more resistant than PDC from Zymomonas mobilis, 8 mM, 2h, stable
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid
-
wild type enzyme and mutant enzymes D28A, H114F, H115F and E477Q
additional information
-
growth on a medium with oxythiamine increases enzyme activity, but may be in response to an earlier inhibition of enzyme leading to an accumulation of pyruvate, which induces the biosynthesis of enzyme apoform
-
additional information
-
dephosphorylation of Pdc1p by alkaline phosphatase inhibits the enzyme activity by 50%
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pyruvamide
the activator pyruvamide arrests one of the flexible loops comprising residues 106-113 and 292-301, so that two of four active sites become closed, the loop of residues 105-113 remains flexible in the nonactivated enzyme, overview
pyruvate
allosteric substrate activation, binding of substrate at a regulatory site induces catalytic activity, accompanied by conformational changes and subunit rearrangements
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
Pyruvamide
-
activates, pyruvate and pyruvamide have different activation pathways with distinct binding sites
Pyruvamide
-
activation mechanism, binds only at the regulatory site, but with lower affinity than does pyruvate
Pyruvamide
-
activator, 2 binding sites per dimer, mode of binding, a disorder-order transition of two active-site loop regions is a key event in the activation process, kinetic data, mechanism
Pyruvamide
-
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
pyruvate
-
allosteric substrate activation, alternating sites mechanism, random binding of pyruvate in the regulatory and active site, regulatory pyruvate is first bound to C-221 on the beta domain, binding generates a signal which is transmitted to the thiamine diphosphate cofactor, signal pathway, study of the pH-dependence of activation, two-step phenomenological model of activation, kinetics, pyruvate and pyruvamide have different activation pathways with distinct binding sites
pyruvate
-
allosteric substrate activation, kinetics of dimeric and tetrameric enzyme
pyruvate
-
hysteretic substrate activation, Cys-221 binds pyruvate to transmit the information to H-92, E-91, W-412, G-413 and finally to the active center thiamine diphosphate
pyruvate
-
substrate activation pathway from C221 to H92 to E91 to W412 to G413 to thiamine diphosphate, role of W412
pyruvate
-
substrate activation pathway, the consequences of binding substrate at C221 are propagated to the active site via the pathway H92 to E91 to W412 to G413 to thiamine diphosphate, role of C221 and E91
pyruvate
-
substrate activation, interaction of pyruvate with residue C221 provides the trigger, transmitting the information along the C221 to H92 to E91 to W412 to G413 pathway to the 4-amino nitrogen of the thiamine diphosphate cofactor, changes in hydrogen bonding at the active center as a result of substrate activation, mechanism
additional information
-
growth on a medium with oxythiamine increases enzyme activity, but may be in response to an earlier inhibition of enzyme leading to an accumulation of pyruvate, which induces the biosynthesis of enzyme apoform
-
additional information
-
glucose induces the enzyme not through a single signalling pathway, but involving several pathways, glucose sensors Gpr1, Snf3 and Rgt2 are not required, mutational analysis, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic data, pH-dependence of steady-state kinetic parameters
-
additional information
additional information
-
kinetic data, pH-dependence of steady-state kinetic parameters of wild-type, W412F and W412A mutant PDC
-
additional information
additional information
-
kinetic model, kinetic data
-
additional information
additional information
-
kinetic model, Km values for different conformations of wild-type enzyme at different pH values between pH 4.5 and 6.5
-
additional information
additional information
-
kinetic parameters for carboligase reactions of wild-type and mutant YPDC
-
additional information
additional information
-
pH-dependent kinetic data of wild-type, C221E/C222A and C221A/C222A double mutant YPDC
-
additional information
additional information
-
pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetic parameters for beta-hydroxypyruvate
-
additional information
additional information
-
transient state, pre-steady-state, and steady-state complex formations of substrate/intermediate and thiamine diphosphate cofactor and of kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat values at different pH values from pH 4.5 to 7.5 of wild-type, W412F and W412A mutant PDC
-
additional information
additional information
-
kcat values of wild-type, C221E/C222A and C221A/C222A double mutant YPDC at different pH values between pH 5 and 7.2
-
additional information
additional information
-
kinetic model, kcat values for different conformations of wild-type enzyme at different pH values between pH 4.5 and 6.5
-
additional information
additional information
-
kinetic parameters for carboligase reactions of wild-type and mutant YPDC
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
51
phosphate
-
mutant enzyme A143T/T156A/Q367H/N396I/K478R, at pH 6.0 and 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
0.3
-
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
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
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
43.4
-
using pyruvate as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
5.3
-
using 2-oxohexanoic acid as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
6.9
-
using 3-methyl-2-oxobutanoate as substrate, in 100 mM potassium phosphate buffer pH 6.5, 5 mM MgSO4, 0.1 mM thiamine diphosphate
additional information
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
-
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
-
activity in cell extracts grown on different media estimated with and without exogenous thiamine diphosphate
additional information
-
carboligase reaction, wild-type and mutant YPDC, at different pH values
additional information
-
no difference in specific activity of dimeric and tetrameric enzyme state
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
additional information
-
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
8
-
synthesis of L-norephedrine in a coupled reaction with omega-transaminase from Vibrio fluvialis JS17
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.2
-
nearly identical Vmax values in the pH range, wild-type YPDC
7
-
wild-type YPDC forms more acetaldehyde at higher pH, followed by a decrease above pH 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
40
-
enzyme modified with the N-succinimide ester of an amylose glycylglycine adduct
45
30
-
the optimal temperature for Pdc1 activity is dependent upon pyruvate concentration, in 1 mM pyruvate, native Pdc1 performs optimally at 30°C
30
-
synthesis of L-norephedrine in a coupled reaction with omega-transaminase from Vibrio fluvialis JS17
45
-
the optimal temperature for Pdc1 activity is dependent upon pyruvate concentration, in 25 mM pyruvate, native activity peaks at 45?C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
-
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
-
growth profile and ethanol production in isozyme knockout strains, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
evolution
-
the enzyme is a member of the superfamily of thiamine diphosphate-dependent enzymes
malfunction
-
deletion of the Ser/Thr protein phosphatase SIT4 phosphatase decreases the pyruvate decarboxylase activity
metabolism
-
pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeast Saccharomyces cerevisiae, mechanism of regulation of pyruvate decarboxylase activity, overview
physiological function
physiological function
roles of the three isozymes at different phases of Saccharomyces cerevisiae fermentation and with relevance for ethanol and carboligation reactions, overview
physiological function
elimination of pyruvate decarboxylase activity in a pdc1 pdc5 pdc6 triple mutant virtually abolishes isobutyl alcohol production. Any single isozyme of pyruvate decarboxylase is sufficient for the formation of isobutyl alcohol from valine
physiological function
roles of the three isozymes at different phases of Saccharomyces cerevisiae fermentation and with relevance for ethanol and carboligation reactions, overview
physiological function
-
the enzyme is essential for directing the glucose flux to ethanol production. The activity of Pdc1p is regulated by phosphorylation of serine residues during growth
physiological function
elimination of pyruvate decarboxylase activity in a pdc1 pdc5 pdc6 triple mutant virtually abolishes isobutyl alcohol production. Any single isozyme of pyruvate decarboxylase is sufficient for the formation of isobutyl alcohol from valine
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
240000
60000
61320
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
61468
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
61486
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
62000
60000
-
2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
60000
-
4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
60000
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
60000
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
subunit crystal structure analysis, the subunits are each composed of three domains, the R domain, the PYR domain, and the PP domain, all three domains exhibit typical alpha/beta-topology, the enzyme contains flexible loops comprising residues 106-113 and 292-301 involved in catalysis via four active sites, open and closed conformation of the activate and nonactivated enzyme, respectively, the completely open enzyme state is favoured for Saccharomyces cerevisiae pyruvate decarboxylase, overview
dimer or tetramer
-
a tight dimer, known as the functional dimer, is the minimal catalytically active unit, two of these functional dimers assemble into a loose tetramer in the quaternary structure
homodimer
-
2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
homotetramer
monomer
tetramer
additional information
?
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
?
-
x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
homotetramer
-
4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
homotetramer
-
dimer of dimers, minimal catalytic unit is a functional dimer
homotetramer
-
dimer of dimers, minimal catalytic unit is a functional dimer, two active sites in the functional dimer act in an antiphase manner during the reaction, with each active site eventually completing the full catalytic cycle, study of subunit dissociation into two types of dimers depending on the experimental conditions and their reassociation
homotetramer
-
dimer of dimers, the minimal catalytic unit is the dimer with its active sites are not acting independently of one another, alternating sites model
tetramer
-
enzyme structure, differences in the tetramer assembly of form A and B PDC, form A is the native PDC
additional information
-
one isoenzyme has the subunit structure alpha4 and the other has the subunit structure alpha2'beta2
additional information
-
thiamine diphosphate is required for complete association of subunits to form active oligomer
additional information
-
different oligomeric states, tetramers, dimers and monomers, of enzyme occur under defined conditions, unfolding kinetics, tetramers dissociate via a stable dimeric state into monomers
additional information
-
treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
additional information
-
conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
Pdc1p is subject to reversible phosphorylation at Ser223 that is dependent on glucose availability, dephosphorylation of Pdc1p by alkaline phosphatase inhibits the enzyme activity by 50%. Phosphorylation of Pdc1p is dependent on the growth phase, being hyperphosphorylated in the logarithmic phase, dependent on the presence of Ser/Thr protein phosphatase SIT4p. The Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A143T/T156A/Q367H/N396I/K478R
A287G
-
the mutant shows reduced activity compared to the wild type enzyme
C221A
C221A/C222A
C221D/C222A
-
double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics
C221E/C222A
C221S
C222A
-
still possesses 20-30% specific activity compared to the wild type enzyme and can still be inhibited by the (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid class of inhibitors/substrate analogues as well as cinnamaldehydes
D28A
D28N
D291A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
D291N
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced activity compared to the wild-type enzyme
E477Q
E51A
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme,and the mutant is no longer capable of forming a hydrogen bond with cofactor thiamine diphosphate
E51D
E51N
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E51Q
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E91A
-
mutant with 30fold reduced specific activity, reduced turnover number and catalytic efficiency, abolished cooperativity, reduced thermal stability, impaired ability to bind the cofactors
E91D
E91Q
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency, abolished cooperativity, reduced thermal stability, impaired ability to bind the cofactors
H114F
H115F
H225F
-
the mutant shows reduced activity compared to the wild type enzyme
H310F
-
the mutant shows reduced activity compared to the wild type enzyme
L111A
-
site-directed mutagenesis, the mutant shows 47% of the wild-type kcat
L111Q
-
site-directed mutagenesis, the mutant shows 73% of the wild-type kcat
L111V
-
site-directed mutagenesis, the mutant shows 21% of the wild-type kcat
N293A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
S298A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
S300A
-
site-directed mutagenesis, the mutant shows altered kinetics with slightly reduced kcat compared to the wild-type enzyme
S311A
-
the mutant shows reduced activity compared to the wild type enzyme
T294A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
W412A
-
mutant with 10fold reduced specific activity, reduced turnover number and catalytic efficiency, very much reduced substrate activation, reduced affinity for thiamine diphosphate, reduced stability
W412F
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency
additional information
A143T/T156A/Q367H/N396I/K478R
-
mutant shows improved activity for 1 mM pyruvate at pH 7.5 in the presence of phosphate, has the substrate concentration required for half-saturation reduced by almost 3fold at pH 7.5 and the phosphate inhibition reduced by 4fold at pH 6.0 compared to the wild type enzyme, the mutant can be activated by pyruvate more easily than the native enzyme
A143T/T156A/Q367H/N396I/K478R
-
the mutant shows improved activity for 1 mM pyruvate at pH 7.5 in the presence of phosphate. In comparison with native Pdc1, the mutant has the substrate concentration required for half-saturation reduced by almost 3fold at pH 7.5 and the phosphate inhibition reduced by 4fold at pH 6.0, the apparent cooperativity for pyruvate is also reduced since it is activated by pyruvate more easily than the native enzyme
C221A
-
mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6
C221A/C222A
-
active double mutant without substrate activation, effect of modified substrate-activation site on catalysis, kinetic properties
C221A/C222A
-
the mutant shows reduced activity compared to the wild type enzyme
C221E/C222A
-
double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics
C221E/C222A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C221S
-
still possesses 20-30% specific activity compared to the wild type enzyme and can still be inhibited by the (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid class of inhibitors/substrate analogues as well as cinnamaldehydes
C221S
-
mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6
C221S
-
mutant with abolished activation and reduced Hill coefficient
D28A
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
D28A
-
lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction
D28A
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
D28A
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
D28N
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
D28N
-
lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction, higher acetoin formation than by wild-type YPDC
D28N
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
E477Q
-
active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate
E477Q
-
active site mutant, kinetics, activation study of mutant enzyme
E477Q
-
lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction, higher acetoin formation than by wild-type YPDC
E477Q
-
site-directed mutagenesis, the mutant enzyme shows additional carboligation activity
E477Q
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme
E51D
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E91D
-
mutant with 5fold reduced specific activity, reduced turnover number and catalytic efficiency, slightly reduced Hill coefficient, reduced thermal stability, impaired ability to bind the cofactors
E91D
-
racemic C2-alpha-lactylthiamine diphosphate exposed to mutant enzyme is partitioned between reversion to pyruvate and decarboxylation
E91D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
-
growth profile and ethanol production in isozyme knockout strains, overview
additional information
-
construction of mutant pdc-803 with a S296DELTAF297DELTA deletion, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
growth profile and ethanol production in isozyme knockout strains, overview
additional information
-
growth profile and ethanol production in isozyme knockout strains, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
690937
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
705199
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 35
-
half-life of 235 h at 20°C, half-life of 78 h at 30°C, half-life of 62 h at 35°C
45 - 65
-
the activity of native Pdc1 decreases with increasing temperature from 45°C and is completely abolished at 65°C, the temperature at which half of the native Pdc1 activity is irreversibly lost in 5 min is at 52.6°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the highest enzyme activity is in glucose, followed by glycerol, while there is negligible activity on ethanol and methanol as growth medium
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 22°C
-
low stability in the isolated state, less stable than PDC from Zymomonas mobilis
-
the enzyme in phosphate buffer pressurized with CO2 up to 9 MPa for 1 h at 35°C loses most of its activity. Although the residual activity is higher in MES buffer than in phosphate buffer, deactivation cannot be prevented. With 0.7 M glycerol, the residual activity is double that without additives, and with 1-1.2 M trehalose, the residual activity is 1.5times that without additives. The stability of the enzyme is improved dramatically by immobilization onto the ion-exchange polymer Mukouyama 2000, the biocatalytic activity is fully retained even after treatment at 11 MPa. The stability of the enzyme immobilized on Toyonite-200 is lower than that of free enzyme
-
the highest enzyme activity is in glucose, followed by glycerol, while there is negligible activity on ethanol and methanol as growth medium
with about 1 mM pyruvate, native Pdc1 only reaches a stable reaction rate after exposure to pyruvate for 1 min, the N-terminal His tag has no influence on activity of native Pdc1
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
-
treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 10 mM PIPES at pH 6.5 with 1 mM dithiothreitol, 1 mM MgCl2, and 0.1 mM thiamine diphosphate, several weeks, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by acetone precipitation, ammonium sulfate fractionation, and gel filtration to over 95% homogeneity
HisTrap column chromatography, Fractogel EMD TMAE 650S gel filtration, and Superdex 200 gel filtration
-
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, E91A, E91D and E91Q mutant PDC, expressed in Escherichia coli, mutants are purified as apoenzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
subcloning in Escherichia coli strain DH5alpha, expression of C-terminally His-tagged isozymes in Escherichia coli strain BL21(DE3)plysS
expressed in Escherichia coli BL21(DE3)pLysS cells
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
-
subcloning in Escherichia coli strain DH5alpha, expression of C-terminally His-tagged isozymes in Escherichia coli strain BL21(DE3)plysS
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
COMMENTARY
LITERATURE
synthesis
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
-
modification of enzyme with the N-succinimide ester of an amylose glycylglycine adduct. Upon conjugation, the optimum temperature shifts from 35°C to 40°C, the conjugate shows higher resistance to heat treatment than the native enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuo, D.J.; Dikdan, G.; Jordan, F.
Resolution of brewers' yeast pyruvate decarboxylase into two isozymes
J. Biol. Chem.
261
3316-3319
1986
Saccharomyces cerevisiae
Chen, G.C.; Jordan, F.
Brewers' yeast pyruvate decarboxylase produces acetoin from acetaldehyde: a novel tool to study the mechanism of steps subsequent to carbon dioxide loss
Biochemistry
23
3576-3582
1984
Saccharomyces cerevisiae
Knig, S.; Hubner, G.; Schellenberger, A.
Cross-linking of pyruvate decarboxylase. Characterization of the native and substrate-activated enzyme states
Biomed. Biochim. Acta
49
465-471
1990
Saccharomyces cerevisiae
Gounaris, A.D.; Turkenkopf, I.; Civerchia, L.L.; Greenlie, J.
Pyruvate decarboxylase III. Specificity restrictions for thiamine pyrophosphate in the protein association step, sub-unit structure
Biochim. Biophys. Acta
405
492-499
1975
Saccharomyces cerevisiae
Ludewig, R.; Schellenberger, A.
A new procedure to prepare highly purified and crystallized yeast pyruvate decarboxylase
FEBS Lett.
45
340-343
1974
Saccharomyces cerevisiae
Candy, J.M.; Duggleby, R.G.
Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme
Biochim. Biophys. Acta
1385
323-338
1998
Acetobacter sp., Aspergillus sp., Saccharomyces cerevisiae, Canavalia ensiformis, Citrus sp., Clostridium botulinum, Erwinia amylovora, Hanseniaspora uvarum, Ipomoea batatas, Kluyveromyces sp., Neurospora crassa, Pastinaca sativa, Pisum sativum, Saccharomyces pastorianus, Saccharomyces uvarum, Sarcina ventriculi, Schizosaccharomyces pombe, Zea mays, Zymomonas mobilis
Baburina, I.; Dikdan, G.; Guo, F.; Tous, G.I.; Root, B.; Jordan, F.
Reactivity at the substrate activation site of yeast pyruvate decarboxylase: inhibition by distortion of domain interactions
Biochemistry
37
1245-1255
1998
Saccharomyces cerevisiae
Killenberg-Jabs, M.; Koenig, S.; Hohmann, S.; Hubner, G.
Purification and characterization of the pyruvate decarboxylase from a haploid strain of Saccharomyces cerevisiae
Biol. Chem. Hoppe-Seyler
377
313-317
1996
Saccharomyces cerevisiae
Li, H.; Jordan, F.
Effects of substitution of tryptophan 412 in the substrate activation pathway of yeast pyruvate decarboxylase
Biochemistry
38
10004-10012
1999
Saccharomyces cerevisiae
Li, H.; Furey, W.; Jordan, F.
Role of glutamate 91 in information transfer during substrate activation of yeast pyruvate decarboxylase
Biochemistry
38
9992-10003
1999
Saccharomyces cerevisiae
Wang, J.; Golbik, R.; Seliger, B.; Spinka, M.; Tittmann, K.; Hubner, G.; Jordan, F.
Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase
Biochemistry
40
1755-1763
2001
Saccharomyces cerevisiae, Zymomonas mobilis
Sergienko, E.A.; Jordan, F.
Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products
Biochemistry
40
7369-7381
2001
Saccharomyces cerevisiae
Sergienko, E.A.; Jordan, F.
Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values
Biochemistry
40
7382-7403
2001
Saccharomyces cerevisiae
Sergienko, E.A.; Jordan, F.
New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme
Biochemistry
41
3952-3967
2002
Saccharomyces cerevisiae
Wei, W.; Liu, M.; Jordan, F.
Solvent kinetic isotope effects monitor changes in hydrogen bonding at the active center of yeast pyruvate decarboxylase concomitant with substrate activation: the substituent at position 221 can control the state of activation
Biochemistry
41
451-461
2002
Saccharomyces cerevisiae
Sergienko, E.A.; Jordan, F.
Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants, with substitution of adjacent active center acidic groups from different subunits, display restored activity
Biochemistry
41
6164-6169
2002
Saccharomyces cerevisiae
Hajipour, G.; Schowen, K.B.; Schowen, R.L.
The linkage of catalysis and regulation in enzyme action: oxidative diversion in the hysteretically regulated yeast pyruvate decarboxylase
Bioorg. Med. Chem.
7
887-894
1999
Saccharomyces cerevisiae
Killenberg-Jabs, M.; Kern, G.; Hubner, G.; Golbik, R.
Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase
Biophys. Chem.
96
259-271
2002
Saccharomyces cerevisiae
Goetz, G.; Iwan, P.; Hauer, B.; Breuer, M.; Pohl, M.
Continuous production of (R)-phenylacetylcarbinol in an enzyme-membrane reactor using a potent mutant of pyruvate decarboxylase from Zymomonas mobilis
Biotechnol. Bioeng.
74
317-325
2001
Saccharomyces cerevisiae, Zymomonas mobilis
Lu, G.; Dobritzsch, D.; Baumann, S.; Schneider, G.; Konig, S.
The structural basis of substrate activation in yeast pyruvate decarboxylase. A crystallographic and kinetic study
Eur. J. Biochem.
267
861-868
2000
Saccharomyces cerevisiae, Saccharomyces cerevisiae WS34/70
Killenberg-Jabs, M.; Jabs, A.; Lilie, H.; Golbik, R.; Hubner, G.
Active oligomeric states of pyruvate decarboxylase and their functional characterization
Eur. J. Biochem.
268
1698-1704
2001
Saccharomyces cerevisiae
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