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Literature summary for 4.1.1.1 extracted from

  • Wang, J.; Dong, H.; Li, S.; He, H.
    Theoretical study toward understanding the catalytic mechanism of pyruvate decarboxylase (2005), J. Phys. Chem. B, 109, 18664-18672.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Reaction

Reaction Comment Organism Reaction ID
a 2-oxo carboxylate = an aldehyde + CO2 Glu51 is the most important residue in formation of the ylide and the release of acetaldehyde. Glu477 and Asp28 are involved in decarboxylation of lactylthiamine diphosphate. Protonation of alpha-carbanion to form 2-(1-hydroxyethyl)-thiamine diphosphate goes through a concerted double proton transfer transition state involving both Asp28 and His115. Decarboxylation of lactylthiamine diphosphate and protonation of alpha-carbanion are two rate-limiting steps Saccharomyces cerevisiae