Structural Basis for Catalysis by the Mono- and Dimetalated Forms of the dapE-Encoded N-succinyl-l,l-Diaminopimelic Acid Desuccinylase-Reference-Cited by-同舟云学术

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Structural Basis for Catalysis by the Mono- and Dimetalated Forms of the dapE-Encoded N-succinyl-l,l-Diaminopimelic Acid Desuccinylase

Published:2010-04 Issue:3 Volume:397 Page:617-626
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Nocek Boguslaw P.,Gillner Danuta M.,Fan Yao,Holz Richard C.,Joachimiak Andrzej

Funder

National Science Foundation

National Institutes of Health

U.S. Department of Energy, Office of Biological and Environmental Research

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference49 articles.

1. Enzymology of bacterial lysine biosynthesis;Scapin;Adv. Enzymol.,1998

2. Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis;Born;Curr. Opin. Chem. Biol.,1999

3. The lysine pathway as a target for a new genera of synthetic antibacterial antibiotics?;Girodeau;J. Med. Chem.,1986

4. Characterization of Helicobacter pylori dapE and construction of a conditionally lethal dapE mutant;Karita;Infect. Immun.,1997

5. Biosynthesis of diaminopimelate, the precursor of lysine and a component of peptidoglycan, is an essential function of Mycobacterium smegmatis;Pavelka;J. Bacteriol.,1996

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