This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1jje
From Proteopedia
|
IMP-1 METALLO BETA-LACTAMASE FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH A BIARYL SUCCINIC ACID INHIBITOR (11)
Overview
IMP-1 metallo-beta-lactamase (class B) is a plasmid-borne zinc, metalloenzyme that efficiently hydrolyzes beta-lactam antibiotics, including carbapenems, rendering them ineffective. Because IMP-1 has been, found in several clinically important carbapenem-resistant pathogens, there is a need for inhibitors of this enzyme that could protect broad, spectrum antibiotics such as imipenem from hydrolysis and thus extend, their utility. We have identified a series of 2,3-(S,S)-disubstituted, succinic acids that are potent inhibitors of IMP-1. Determination of high, resolution crystal structures and molecular modeling of succinic acid, inhibitor complexes with IMP-1 has allowed an understanding of the, potency, stereochemistry, and structure-activity relationships of these, inhibitors.
About this Structure
1JJE is a Single protein structure of sequence from Pseudomonas aeruginosa with ZN, ACT and BYS as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase., Toney JH, Hammond GG, Fitzgerald PM, Sharma N, Balkovec JM, Rouen GP, Olson SH, Hammond ML, Greenlee ML, Gao YD, J Biol Chem. 2001 Aug 24;276(34):31913-8. Epub 2001 Jun 4. PMID:11390410
Page seeded by OCA on Tue Nov 20 18:19:27 2007
