UNSPECIFIED (2003) Synthesis and activity of 5'-uridinyl dipeptide analogues mimicking the amino terminal peptide chain of nucleoside antibiotic mureidomycin A. BIOORGANIC & MEDICINAL CHEMISTRY, 11 (14). pp. 3083-3099. ISSN 0968-0896

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Abstract

A series of 5'-uridinyl dipeptides were synthesised which mimic the amino terminal chain of nucleoside antibiotic mureido omycin A. Aminoacyl-beta-alanyl- and aminoacyl-N-methyl-beta-alanyl- dipeptides were attached either via an ester linkage to the 5'-hydroxyl of uridine. or via an amide linkage to 5-amino-5-deoxyuridine. The most active inhibitor of Escherichia coli phosphoMurNAc-pentapeptide translocase (MraY) was 5'-O-((L)-Ala-N-methyl-beta-alanyl)-uridine (131), which also showed 97% enzyme inhibition at 2.35mM concentration, and showed antibacterial activity at 100 mug/mL concentration against Pseudomonas putida. Both the central N-methyl amide linkage and a 5' uridine ester linkage were required for highest biological activity. Enzyme inhibition was shown to be competitive with Mg2+. It is proposed that the primary amino terminus of the inhibitor binds in place of the Mg2+. cofactor at the MraY active site, positioned via a cis-N-methyl amide linkage. (C) 2003 Elsevier Science Ltd. All rights reserved.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	BIOORGANIC & MEDICINAL CHEMISTRY
Publisher:	PERGAMON-ELSEVIER SCIENCE LTD
ISSN:	0968-0896
Date:	17 July 2003
Volume:	11
Number:	14
Number of Pages:	17
Page Range:	pp. 3083-3099
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/9625

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