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Cover Picture: Mechanistic Insights into Cyclooxygenase Irreversible Inactivation by Aspirin (ChemMedChem 6/2009)
Author(s) -
Tosco Paolo,
Lazzarato Loretta
Publication year - 2009
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200990026
Subject(s) - moiety , chemistry , aspirin , stereochemistry , mutagenesis , carboxylate , acetylation , cyclooxygenase , cover (algebra) , biochemistry , enzyme , mutation , mechanical engineering , engineering , gene
Abstract The cover picture shows aspirin docked in the active site of ovine COX‐1. According to the results of this QM/MM study, this is the conformation likely to trigger Ser 530 acetylation under general base catalysis by the carboxylate group of aspirin. The hydroxy group of Tyr 385 proved to play a key role in orienting and polarizing the acetyl moiety, as previously postulated by Hochgesang et al. on the basis of site‐directed mutagenesis experiments. For more details, see the Communication by P. Tosco and L. Lazzarato on p. 939 ff.