Literature DB >> 9871517

Peptide inhibitors of N-succinyl diaminopimelic acid aminotransferase (DAP-AT): a novel class of antimicrobial compounds.

R J Cox1, J A Schouten, R A Stentiford, K J Wareing.   

Abstract

Dipeptide substrates of N-Succinyl Diaminopimelic Acid Aminotransferase (DAP-AT) were converted to hydrazines by treatment with hydrazine and cyanoborohydride. These compounds were tested in vitro as inhibitors of DAP-AT from E. coli and in vivo as antibiotics. The hydrazino-dipeptides showed potent slow binding slow binding inhibition of DAP-AT as well as antimicrobial activity.

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Year:  1998        PMID: 9871517     DOI: 10.1016/s0960-894x(98)00149-8

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  1 in total

1.  Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapC (Rv0858c) from Mycobacterium tuberculosis.

Authors:  Simone Weyand; Georgia Kefala; Manfred S Weiss
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-07-25
  1 in total

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