We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments A thiamine-diphosphate protein. Also catalyses acyloin formation.
The taxonomic range for the selected organisms is: Kluyveromyces lactis The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
pdc, pyruvate decarboxylase, acetohydroxyacid synthase, yeast pyruvate decarboxylase, pdc1p, p59nc, ifpl730, zmpdc, pyruvate decarboxylase 1, pdc5p,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8-10 nm cytoplasmic filament-associated protein
-
-
-
-
alpha-Carboxylase
-
-
-
-
alpha-Keto acid carboxylase
-
-
-
-
Decarboxylase, pyruvate
-
-
-
-
Pyruvic decarboxylase
-
-
-
-
PDC
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a 2-oxo carboxylate = an aldehyde + CO2
catalytic mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxo-acid carboxy-lyase (aldehyde-forming)
A thiamine-diphosphate protein. Also catalyses acyloin formation.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyruvate
acetaldehyde + CO2
pyruvate
acetaldehyde + CO2
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
catalytic cycle, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, contains catalytic and regulatory pyruvate binding site
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
thiamine diphosphate
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of the cofactor at pH above 8.0, leads to complete loss of activity
thiamine diphosphate
-
-
thiamine diphosphate
-
requirement
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Mg2+
dependent on, bound tightly, but not covalently, at the interface of two monomers, reversible dissociation of Mg2+ at pH above 8.0, leads to complete loss of activity
Mg2+
-
cofactor, requirement
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Pyruvamide
-
mixed type inhibitor
pyruvate
-
weak substrate inhibition, above 100 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Pyruvamide
the activator pyruvamide arrests the flexible loops comprising residues 106-113 and 292-301, so that two of four active sites become closed
pyruvate
allosteric substrate activation, binding of substrate at a regulatory site induces catalytic activity, accompanied by conformational changes and subunit rearrangements, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process
Pyruvamide
-
artificial activator
pyruvate
-
concentration-dependent substrate activation, minimum at 1.5 mM, mechanism, kinetics
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.24
pyruvate
-
pH 6, 30°C
additional information
additional information
-
kinetic studies
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40
pyruvate
-
pH 6, 30°C, enzyme monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1200
pyruvate
-
pH 6, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
single gene
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
200000
-
about, gel filtration
61500
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
61821
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
tetramer
subunit crystal structure analysis, the subunits are each composed of three domains, the R domain, the PYR domain, and the PP domain, all three domains exhibit typical alpha/beta-topology, the enzyme shows a half-side closed tetramer in presence or absence of any activator, the half-side closed form is predominant for Kluyveromyces lactis pyruvate decarboxylase, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process, overview
tetramer
-
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
purified recombinant enzyme, 2 mg/ml protein in 50 mM MES, pH 6.45, 5 mM thiamine diphosphate, 1 mM dithiothreitol, and 5 mM MgSO4, or 35 mM sodium citrate, pH 6.45, 1 mM dithiothreitol, 5 mM thiamine diphosphate, and 5 mM MgSO4, in absence of ammonium sulfate, hanging drop vapour diffusion method, 8°C, in a 1:1 mixture with reservoir solution containing 20% w/v PEG 2000/PEG 8000 in crystallization buffer, microcrystals within 3 days, larger crystals within 4 weeks, X-ray diffraction structure determination and analysis at 2.26 A resolution
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)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D28A
-
the mutant is almost catalytically inactive
E477Q
-
the mutant is almost catalytically inactive
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
native enzyme by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography to over 95% homogeneity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Hansenula polymorpha
-
expressed in Hansenula polymorpha strain NCYC495 leu1-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Krieger, F.; Spinka, M.; Golbik, R.; Hubner, G.; Konig, S.
Pyruvate decarboxylase from Kluyveromyces lactis. An enzyme with an extraordinary substrate activation behaviour
Eur. J. Biochem.
269
3256-3263
2002
Kluyveromyces lactis, Kluyveromyces lactis JA-6
brenda
Kutter, S.; Wille, G.; Relle, S.; Weiss, M.S.; Huebner, G.; Koenig, S.
The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis. Implications for the substrate activation mechanism of this enzyme
FEBS J.
273
4199-4209
2006
Saccharomyces cerevisiae (P06169), Saccharomyces cerevisiae, Kluyveromyces lactis (Q12629), Kluyveromyces lactis
brenda
Ishchuk, O.P.; Voronovsky, A.Y.; Stasyk, O.V.; Gayda, G.Z.; Gonchar, M.V.; Abbas, C.A.; Sibirny, A.A.
Overexpression of pyruvate decarboxylase in the yeast Hansenula polymorpha results in increased ethanol yield in high-temperature fermentation of xylose
FEMS Yeast Res.
8
1164-1174
2008
Kluyveromyces lactis, Kluyveromyces lactis CBS 2359
brenda
Kutter, S.; Weiss, M.S.; Wille, G.; Golbik, R.; Spinka, M.; Koenig, S.
Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation
J. Biol. Chem.
284
12136-12144
2009
Kluyveromyces lactis, Saccharomyces cerevisiae (P06169), Saccharomyces cerevisiae
brenda