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

doi:10.1016/j.bmcl.2003.08.082

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 journal › Article › peer-review

31 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 language	English
Pages (from-to)	4489-4492
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	13
Issue number	24
DOIs	https://doi.org/10.1016/j.bmcl.2003.08.082
Publication status	Published - 15 Dec 2003

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title = "Novel mechanism of inhibiting β-Lactamases by sulfonylation using β-Sultams",

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.",

author = "M.I. Page and P.S. Hinchliffe and J.M. Wood and L.P. Harding and A.P. Laws",

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T1 - Novel mechanism of inhibiting β-Lactamases by sulfonylation using β-Sultams

AU - Page, M.I.

AU - Hinchliffe, P.S.

AU - Wood, J.M.

AU - Harding, L.P.

AU - Laws, A.P.

N1 - cited By 27

PY - 2003/12/15

Y1 - 2003/12/15

N2 - 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.

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.

U2 - 10.1016/j.bmcl.2003.08.082

DO - 10.1016/j.bmcl.2003.08.082

M3 - Article

VL - 13

SP - 4489

EP - 4492

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

SN - 0960-894X

IS - 24

ER -

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

Abstract

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