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Literature summary extracted from

  • 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 (2001), Biochemistry, 40, 1755-1763.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.1 additional information not activated by the substrate pyruvate Zymomonas mobilis
4.1.1.1 Pyruvamide artificial activator Saccharomyces cerevisiae
4.1.1.1 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 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.1 C221A/C222A active double mutant without substrate activation, effect of modified substrate-activation site on catalysis, kinetic properties Saccharomyces cerevisiae
4.1.1.1 C221S mutant with abolished activation and reduced Hill coefficient Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.1 additional information
-
 additional information kinetic data Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Saccharomyces cerevisiae
-
-
-
4.1.1.1 Zymomonas mobilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.1 wild-type PDC and C221A/C222A double mutant Saccharomyces cerevisiae

Reaction

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.1 45 50 pH 6, 25°C, wild-type PDC Saccharomyces cerevisiae
4.1.1.1 120
-
-
 Zymomonas mobilis
4.1.1.1 515
-
 pH 6, 25°C, C221A/C222A double mutant PDC Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 pyruvate
-
 Saccharomyces cerevisiae acetaldehyde + CO2
-
 ir
4.1.1.1 pyruvate catalytic mechanism Saccharomyces cerevisiae acetaldehyde + CO2
-
 ir
4.1.1.1 pyruvate H113 is involved in substrate binding and mediates the opening and closing of the active site by ion pairing with the carboxyl group of pyruvate Zymomonas mobilis acetaldehyde + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.1 YPDC
-
 Saccharomyces cerevisiae
4.1.1.1 ZmPDC
-
 Zymomonas mobilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.1 25
-
 assay at Saccharomyces cerevisiae

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.1.1.1 4 30 enzyme is 6times more active at 30°C than at 4°C Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.1 2.5
-
 pyruvate pH 6, 4°C, C221A/C222A double mutant PDC Saccharomyces cerevisiae
4.1.1.1 10
-
 pyruvate pH 6, 4°C, wild-type PDC Saccharomyces cerevisiae
4.1.1.1 15
-
 pyruvate pH 6, 30°C, C221A/C222A double mutant PDC Saccharomyces cerevisiae
4.1.1.1 120
-
 pyruvate
-
 Zymomonas mobilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.1 6
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.1 thiamine diphosphate requirement, mode of active site binding Saccharomyces cerevisiae