Details
| Original language | English |
|---|---|
| Pages (from-to) | 945-950 |
| Number of pages | 6 |
| Journal | Bioorganic and Medicinal Chemistry Letters |
| Volume | 8 |
| Issue number | 8 |
| Publication status | Published - 21 Apr 1998 |
| Externally published | Yes |
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 hydrazinodipeptides showed potent slow binding inhibition of DAP-AT as well as antimicrobial activity.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Medicine
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Pharmacology, Toxicology and Pharmaceutics(all)
- Pharmaceutical Science
- Pharmacology, Toxicology and Pharmaceutics(all)
- Drug Discovery
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
- Chemistry(all)
- Organic Chemistry
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In: Bioorganic and Medicinal Chemistry Letters, Vol. 8, No. 8, 21.04.1998, p. 945-950.
Research output: Contribution to journal › Article › Research › peer review
}
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 -