Layland, Nicola J., Laws, Andrew P., Vilanova, Bartolomé and Page, Michael I. (1995) Penicillin 3-aldehyde is a good substrate and not an inhibitor of ?-lactamases A and C. Journal of the Chemical Society, Perkin Transactions 2 (5). pp. 869-870. ISSN 1472-779X
Metadata only available from this repository.Abstract
Replacement of the 3-carboxylate residue in phenoxymethylpenicillin by an aldehyde group gives a good substrate for E. cloacae P99 -lactamase with kcat= 34 s–1, Km= 7.5 × 10–5 mol dm–3 and kcat/Km= 4.5 × 105 dm3 mol–1 s–1 at pH 7. With B. cereus 569/H -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
Item Type: | Article |
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Subjects: | Q Science > Q Science (General) Q Science > QD Chemistry |
Schools: | School of Applied Sciences |
Related URLs: | |
Depositing User: | Sharon Beastall |
Date Deposited: | 05 Nov 2009 13:21 |
Last Modified: | 28 Aug 2021 10:52 |
URI: | http://eprints.hud.ac.uk/id/eprint/6098 |
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