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Publication Abstract from PubMed
A classical peptide inhibitor of serine proteases that is hydrolyzed approximately 10(7) times more slowly than a good substrate is shown to form an acyl-enzyme intermediate rapidly. Despite this quick first step, further reaction is slowed dramatically because of tight and oriented binding of the cleaved peptide, preventing acyl-enzyme hydrolysis and favoring the reverse reaction. Moreover, this mechanism appears to be common to a large class of tight-binding serine protease inhibitors that mimic good substrates. The arrest of enzymatic reaction at the intermediate stage allowed us to determine that the consensus nucleophilic attack angle is close to 90 degrees in the reactive Michaelis complexes.
A clogged gutter mechanism for protease inhibitors.,Radisky ES, Koshland DE Jr Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10316-21. Epub 2002 Jul 25. PMID:12142461[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Radisky ES, Koshland DE Jr. A clogged gutter mechanism for protease inhibitors. Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10316-21. Epub 2002 Jul 25. PMID:12142461 doi:10.1073/pnas.112332899
