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

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 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

Fingerprint

Cite this

Page, M. I., Hinchliffe, P. S., Wood, J. M., Harding, L. P., & Laws, A. P. (2003). Novel mechanism of inhibiting β-Lactamases by sulfonylation using β-Sultams. Bioorganic and Medicinal Chemistry Letters, 13(24), 4489-4492. https://doi.org/10.1016/j.bmcl.2003.08.082

@article{7a7cd48d262b4dd8898b0868205fb482,

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",

note = "cited By 27",

year = "2003",

month = "12",

day = "15",

doi = "10.1016/j.bmcl.2003.08.082",

language = "English",

volume = "13",

pages = "4489--4492",

journal = "Bioorganic and Medicinal Chemistry Letters",

issn = "0960-894X",

publisher = "Elsevier Limited",

number = "24",

}

TY - JOUR

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 -

Access to Document

10.1016/j.bmcl.2003.08.082Licence: Unspecified

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344308935&doi=10.1016%2fj.bmcl.2003.08.082&partnerID=40&md5=bdfaf378b79e508ae689f3e327ce442f