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Literature summary for 4.1.1.1 extracted from

  • Baburina, I.; Dikdan, G.; Guo, F.; Tous, G.I.; Root, B.; Jordan, F.
    Reactivity at the substrate activation site of yeast pyruvate decarboxylase: inhibition by distortion of domain interactions (1998), Biochemistry, 37, 1245-1255.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Ketomalonate activates Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C221S still possesses 20-30% specific activity compared to the wild type enzyme and can still be inhibited by the (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid class of inhibitors/substrate analogues as well as cinnamaldehydes Saccharomyces cerevisiae
C222A still possesses 20-30% specific activity compared to the wild type enzyme and can still be inhibited by the (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid class of inhibitors/substrate analogues as well as cinnamaldehydes Saccharomyces cerevisiae
D28A inactivated faster than the wild type enzyme Saccharomyces cerevisiae
E477Q inactivated faster than the wild type enzyme Saccharomyces cerevisiae
H114F inactivated faster than the wild type enzyme Saccharomyces cerevisiae
H115F inactivated faster than the wild type enzyme Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
(E)-4-(4-Chlorophenyl)-2-oxo-3-butenoic acid wild type enzyme and mutant enzymes D28A, H114F, H115F and E477Q Saccharomyces cerevisiae
glyoxalate mechanism-based inhibitor Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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