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2p9v
From Proteopedia
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(New page: 200px<br /><applet load="2p9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p9v, resolution 1.80Å" /> '''Structure of AmpC be...)
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Revision as of 11:21, 21 November 2007
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Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor
Overview
O-Aryloxycarbonyl hydroxamates represent a new class of beta-lactamase, inhibitors. N-Benzyloxycarbonyl-O-(phenoxycarbonyl) hydroxylamine, for, example, inactivates the class C Enterobacter cloacae P99 beta-lactamase, with a rate constant of 6.1 x 103 s-1 M-1; approximately two turnover, events accompany the inhibition., N-Benzyloxycarbonyl-O-[(3-carboxyphenoxy)carbonyl] hydroxylamine is, comparably effective. These compounds also inactivate the class A TEM, beta-lactamase. A crystal structure of the inactivated AmpC enzyme, another class C beta-lactamase, reveals that the active site has become, cross-linked by a carbamate bridge spanning Ser64, the active site, nucleophile, and Lys315, a conserved active site residue.
About this Structure
2P9V is a Protein complex structure of sequences from Escherichia coli with PO4 as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
O-Aryloxycarbonyl Hydroxamates: New beta-Lactamase Inhibitors That Cross-Link the Active Site., Wyrembak PN, Babaoglu K, Pelto RB, Shoichet BK, Pratt RF, J Am Chem Soc. 2007 Aug 8;129(31):9548-9. Epub 2007 Jul 12. PMID:17628063
Page seeded by OCA on Wed Nov 21 13:28:29 2007
