Novel mechanism of inhibiting β-Lactamases by sulfonylation using β-Sultams

M.I. Page, P.S. Hinchliffe, J.M. Wood, L.P. Harding, A.P. Laws

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

β-Sultams are the sulfonyl analogues of β-lactams and N-acyl β-sultams are novel inactivators of the class C β-lactamase of Enterobacter cloacae P99. The rates of inactivation show a similar pH-rate dependence as that exhibited by the β-lactam antibiotics and with ESIMS data it is suggested that β-sultams sulfonylate the active site serine residue to form a sulfonate ester.

β-Sultams inactivate a class C β-lactamase by sulfonylation of the active site serine.
Original languageEnglish
Pages (from-to)4489-4492
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume13
Issue number24
DOIs
Publication statusPublished - 15 Dec 2003

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Lactams
Serine
Catalytic Domain
Enterobacter cloacae
Esters
Anti-Bacterial Agents
naphthosultone

Cite this

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abstract = "β-Sultams are the sulfonyl analogues of β-lactams and N-acyl β-sultams are novel inactivators of the class C β-lactamase of Enterobacter cloacae P99. The rates of inactivation show a similar pH-rate dependence as that exhibited by the β-lactam antibiotics and with ESIMS data it is suggested that β-sultams sulfonylate the active site serine residue to form a sulfonate ester.β-Sultams inactivate a class C β-lactamase by sulfonylation of the active site serine.",
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Novel mechanism of inhibiting β-Lactamases by sulfonylation using β-Sultams. / Page, M.I.; Hinchliffe, P.S.; Wood, J.M.; Harding, L.P.; Laws, A.P.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 13, No. 24, 15.12.2003, p. 4489-4492.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Hinchliffe, P.S.

AU - Wood, J.M.

AU - Harding, L.P.

AU - Laws, A.P.

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AB - β-Sultams are the sulfonyl analogues of β-lactams and N-acyl β-sultams are novel inactivators of the class C β-lactamase of Enterobacter cloacae P99. The rates of inactivation show a similar pH-rate dependence as that exhibited by the β-lactam antibiotics and with ESIMS data it is suggested that β-sultams sulfonylate the active site serine residue to form a sulfonate ester.β-Sultams inactivate a class C β-lactamase by sulfonylation of the active site serine.

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DO - 10.1016/j.bmcl.2003.08.082

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