TY - JOUR

T1 - Peptide inhibitors of N-succinyl diaminopimelic acid aminotransferase (DAP-AT)

T2 - A novel class of antimicrobial compounds

AU - Cox, Russell J.

AU - Schouten, James A.

AU - Stentiford, Rosie A.

AU - Wareing, Katrina J.

N1 - Funding information: Acknowledgement. The authors thank the School of Chemistry, University of Bristol, for financial support. The Nuffield Foundation generously made available an Undergraduate Research Bursary (to JAS, NUF-URB97) and The Royal Society is gratefully thanked for the provision of an academic equipment grant (to tLIC).

PY - 1998/4/21

Y1 - 1998/4/21

N2 - 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 hydrazinodipeptides showed potent slow binding inhibition of DAP-AT as well as antimicrobial activity.

AB - 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 hydrazinodipeptides showed potent slow binding inhibition of DAP-AT as well as antimicrobial activity.

UR - http://www.scopus.com/inward/record.url?scp=0032554693&partnerID=8YFLogxK

U2 - 10.1016/S0960-894X(98)00149-8

DO - 10.1016/S0960-894X(98)00149-8

M3 - Article

C2 - 9871517

AN - SCOPUS:0032554693

VL - 8

SP - 945

EP - 950

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

SN - 0960-894X

IS - 8

ER -