4.1.1.1: pyruvate decarboxylase
This is an abbreviated version!
For detailed information about pyruvate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.1
-
4.1.1.1
-
dendritic
-
plasmacytoid
-
toll-like
-
thiamin
-
claim
-
autoimmune
-
prescript
-
ifn-alpha
-
pharmacy
-
lymphoid
-
herbicide
-
zymomonas
-
branched-chain
-
cdc
-
acetaldehyde
-
mobilis
-
sulfonylurea
-
real-world
-
tregs
-
adhes
-
interferon-alpha
-
insurance
-
lupus
-
antigen-presenting
-
statin
-
costimulatory
-
lipoylated
-
erythematosus
-
nonadherence
-
refill
-
medicare
-
tolerogenic
-
dabigatran
-
acetolactate
-
marketscan
-
dispensing
-
synthesis
-
hla-dr
-
antimitochondrial
-
acetoin
-
dihydrolipoyl
-
biotechnology
-
pharmacist
-
herbicide-resistant
-
beneficiaries
-
icd-9-cm
-
dihydrolipoamide
-
transacetylase
-
rivaroxaban
-
dichloroacetate
-
enrollees
-
lipoate
- 4.1.1.1
- dendritic
-
plasmacytoid
-
toll-like
- thiamin
-
claim
- autoimmune
-
prescript
- ifn-alpha
-
pharmacy
-
lymphoid
-
herbicide
- zymomonas
-
branched-chain
- cdc
- acetaldehyde
- mobilis
- sulfonylurea
-
real-world
-
tregs
-
adhes
- interferon-alpha
-
insurance
-
lupus
-
antigen-presenting
- statin
-
costimulatory
-
lipoylated
- erythematosus
-
nonadherence
-
refill
-
medicare
-
tolerogenic
- dabigatran
- acetolactate
-
marketscan
-
dispensing
- synthesis
-
hla-dr
-
antimitochondrial
- acetoin
-
dihydrolipoyl
- biotechnology
-
pharmacist
-
herbicide-resistant
-
beneficiaries
-
icd-9-cm
- dihydrolipoamide
- transacetylase
- rivaroxaban
- dichloroacetate
-
enrollees
- lipoate
Reaction
Synonyms
2-oxo acid carboxylyase, 8-10 nm cytoplasmic filament-associated protein, acetohydroxyacid synthase, AHAS, alpha-Carboxylase, alpha-Keto acid carboxylase, ANC27, bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase, Decarboxylase, pyruvate, GPDC1, IFPL730, KivD, KlPDC, KviD, NcPDC, P59NC, PDC, PDC I, PDC II, PDC1, Pdc1p, PDC2, PDC3, PDC4, Pdc5, Pdc5p, Pdc6, PDCS.c., PDCZ.m., PDHC, POR, pyruvamide-activated yeast pyruvate decarboxylase, pyruvate decarboxylase, pyruvate decarboxylase 1, pyruvate decarboxylase 2, pyruvate decarboxylase complex, Pyruvic decarboxylase, R-selective pyruvate decarboxylase, SCPDC, scpdc1, ScPDC5, TTHA1213, yeast pyruvate decarboxylase, YPDC, ZbPDC, ZmPDC
ECTree
4.1.1.1 pyruvate decarboxylaseAdvanced search results
results (
results (KM Value
KM Value on EC 4.1.1.1 - pyruvate decarboxylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2.2
2-ketobutyric acid
-
in 100 mM MES buffer (pH 5.6), 5 mM MgCl2, 1 mM dithiothreitol, and 1 mM thiamine diphosphate, at 25°C
0.042
pyruvate
-
in 100 mM MES buffer (pH 5.6), 5 mM MgCl2, 1 mM dithiothreitol, and 1 mM thiamine diphosphate, at 25°C
0.15
pyruvate
-
mutant enzyme E473D, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.31
pyruvate
-
wild type enzyme, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
0.4
pyruvate
-
mutant enzyme E473Q, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate
1.73
pyruvate
pH 6, 25°C, sigmoidal dependence of the reaction rate from substrate concentration, Hill coefficient 2.10
2.5
pyruvate
-
in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
2.8
pyruvate
pH 6.5, potassium MES buffer, two affinities for pyruvate, sigmoidal kinetics
2.8
pyruvate
-
in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate
10
pyruvate
pH 6.5, sodium hydrogen maleate buffer, two affinities for pyruvate, sigmoidal kinetics
additional information
additional information
-
kinetic data, kinetic model
-
additional information
additional information
-
kinetic data, pH-dependence of steady-state kinetic parameters
-
additional information
additional information
-
kinetic data, pH-dependence of steady-state kinetic parameters of wild-type, W412F and W412A mutant PDC
-
additional information
additional information
-
kinetic model, kinetic data
-
additional information
additional information
-
kinetic model, Km values for different conformations of wild-type enzyme at different pH values between pH 4.5 and 6.5
-
additional information
additional information
-
kinetic parameters for carboligase reactions of wild-type and mutant YPDC
-
additional information
additional information
-
pH-dependent kinetic data of wild-type, C221E/C222A and C221A/C222A double mutant YPDC
-
additional information
additional information
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle
-
additional information
additional information
-
values for several C-terminal deletion mutants, kinetic model of the catalytic cycle
-
additional information
additional information
-
kinetics analysis of the wild-type enzyme with beta-hydroxypyruvate as substrate in the decarboxylation reaction
-
additional information
additional information
-
pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetic parameters for beta-hydroxypyruvate
-
additional information
additional information
the isozyme shows sigmoidal kinetics with a Hill coefficient of 1.8
-
additional information
additional information
the isozyme shows sigmoidal kinetics with a Hill coefficient of 1.8
-
additional information
additional information
-
binding affinity of CoA is 0.11 mM
-
additional information
additional information
-
steady-state kinetic analysis, overview. The v/[S] plots display negative cooperativity and hence deviate from Michaelis-Menten kinetics in just the opposite way
-
additional information
additional information
-
the recombinant enzyme expressed in Geobacillus thermoglucosidasius shows normal Michaelis-Menten kinetics with pyruvate
-
additional information
additional information
-
transient state, pre-steady-state, and steady-state complex formations of substrate/intermediate and thiamine diphosphate cofactor and of kinetics of wild-type and mutant enzymes, overview
-
