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Literature summary for 4.1.1.1 extracted from

  • 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 (2002), Biochemistry, 41, 451-461.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Pyruvamide activates Saccharomyces cerevisiae
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 Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C221A active mutant with reduced Hill coefficient of 1 Saccharomyces cerevisiae
C221A/C222A active double mutant, effect on transition states Saccharomyces cerevisiae
C221D/C222A double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics Saccharomyces cerevisiae
C221E/C222A double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics Saccharomyces cerevisiae
C221S active mutant with reduced Hill coefficient of 0.8-0.9 Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
Pyruvamide inhibits at high concentrations Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information pH-dependent kinetic data of wild-type, C221E/C222A and C221A/C222A double mutant YPDC Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence Saccharomyces cerevisiae
61486
-
x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate Saccharomyces cerevisiae
-
acetaldehyde + CO2
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type, C221E/C222A and C221A/C222A double mutant YPDC Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
a 2-oxo carboxylate = an aldehyde + CO2 mechanism Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
-
Saccharomyces cerevisiae acetaldehyde + CO2
-
?
pyruvate mechanism Saccharomyces cerevisiae acetaldehyde + CO2
-
ir

Subunits

Subunits Comment Organism
? x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
YPDC
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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 Saccharomyces cerevisiae
0.99
-
pyruvate pH 6, 25°C, C221E/C222A double mutant YPDC Saccharomyces cerevisiae
3.8
-
pyruvate pH 6, 25°C, C221D/C222A double mutant YPDC Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate requirement, active center, at the interface of the alpha and gamma domains Saccharomyces cerevisiae