Penicillin 3-aldehyde is a good substrate and not an inhibitor of β-lactamases A and C

Nicola J. Layland, Andrew P. Laws, Bartolomé Vilanova, Michael I. Page

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Abstract

Replacement of the 3-carboxylate residue in phenoxymethylpenicillin by an aldehyde group gives a good substrate for E. cloacae P99 βlactamase with, kcat = 34 s-1, Km = 7.5 × 10-5 mol dm-3 and kcat/Km = 4.5 × 10 5 dm3 mol-1 s-1 at pH 7. With B. cereus 569/H β-lactamase I as a catalyst, kcat/Km = 1.87 × 104 dm3 mol-1 s-1 at pH 7 and shows a bell-shaped dependence on pH with apparent pKas of 4.76 and 9.72. Any close proximity between the penicillin 3-aldehyde and a lysine amino group on the protein does not result in iminine formation and inhibition of the enzyme.

Original languageEnglish
Pages (from-to)869-870
Number of pages2
JournalJournal of the Chemical Society, Perkin Transactions 2
Issue number5
DOIs
Publication statusPublished - 1 Dec 1995

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