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 (Activating Compound
Activating Compound 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
ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
chromate
-
sulfur starvation and chromate treatment induce the expression of Pdc6, PDC6 mRNA level is increased more than 100fold following chromate treatment with toxic doses (0.005, 0.01, and 0.02 mM) but remains unchanged at the lower dose 0.0025 mM
CO2
-
PDC activity increases when fruit is treated with 20% CO2 than when fruit is stored in air
Pyruvamide
the activator pyruvamide arrests the flexible loops comprising residues 106-113 and 292-301, so that two of four active sites become closed
Pyruvamide
-
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
Pyruvamide
the activator pyruvamide arrests one of the flexible loops comprising residues 106-113 and 292-301, so that two of four active sites become closed, the loop of residues 105-113 remains flexible in the nonactivated enzyme, overview
pyruvate
-
concentration-dependent substrate activation, minimum at 1.5 mM, mechanism, kinetics
pyruvate
allosteric substrate activation, binding of substrate at a regulatory site induces catalytic activity, accompanied by conformational changes and subunit rearrangements, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process
pyruvate
-
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
pyruvate
allosteric substrate activation, binding of substrate at a regulatory site induces catalytic activity, accompanied by conformational changes and subunit rearrangements
pyruvate
substrate activator is allosterically bound to enzyme, mechanism
additional information
no substrate activation, PDC activity is regulated in response to growth substrate, highest with lactic acid, lower with ethanol or glycerol, and absent with mannitol
-
additional information
-
no substrate activation, PDC activity is regulated in response to growth substrate, highest with lactic acid, lower with ethanol or glycerol, and absent with mannitol
-
additional information
-
the membrane components in whole cells are sufficient for optimal (R)-phenylacetylcarbinol production and no further surfactant addition is required for optimal performance, in vitro cell debris or cell membrane components enhance the (R)-phenylacetylcarbinol production, overview
-
additional information
-
PDC activity in lowland and upland Cyperus rotundus tubers collected from several locations increases significantly when both ecotypes are subjected to hypoxia for 24 h following germination
-
additional information
-
enhanced PDC activity is observed in the skin tissue of fruit at early maturity stages
-
additional information
-
lack of substrate activation in Neurospora crassa yeast pyruvate decarboxylase species
-
additional information
induction of pdc1 is possibly a longterm response and pdc2 a short term response
-
additional information
-
induction of pdc1 is possibly a longterm response and pdc2 a short term response
-
additional information
-
growth on a medium with oxythiamine increases enzyme activity, but may be in response to an earlier inhibition of enzyme leading to an accumulation of pyruvate, which induces the biosynthesis of enzyme apoform
-
additional information
-
glucose induces the enzyme not through a single signalling pathway, but involving several pathways, glucose sensors Gpr1, Snf3 and Rgt2 are not required, mutational analysis, overview
-
additional information
PDC1 is expressed during aerobic growth on glucose and is upregulated 4fold in response to oxygen limitation, PDC1 expression is lower in cells grown on ethanol and succinate than on glucose and is up regulated 2-4fold, respectively, after glucose addition
-
additional information
-
PDC1 is expressed during aerobic growth on glucose and is upregulated 4fold in response to oxygen limitation, PDC1 expression is lower in cells grown on ethanol and succinate than on glucose and is up regulated 2-4fold, respectively, after glucose addition
-
additional information
-
high glycolytic and ethanologenic fluxes correlate with enhanced transcription and enzymatic activity levels of PDC
-
additional information
-
PDC activity in KO11 is limiting and hence positively controls the flux to ethanol formation, since a 7fold amplification of its activity causes a 1.3fold increase into the ethanol flux, increased PDC activity stimulates glucose and xylose consumption rates
-
