Abstract
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 | |
| Publication status | Published - 15 Dec 2003 |
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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 journal › Article
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 -