Accession Number : ADP008368

Title :   Conformational Studies of Boc-L-Pro-L-Pra-Gly-OMe by X-Ray,

Corporate Author : TUEBINGEN UNIV (GERMANY F R)

Personal Author(s) : Hemmasi, B. ; Willisch, H. ; Hiller, W. ; Bayer, E.

Report Date : 1992

Pagination or Media Count : 2

Abstract : L-Propargylglycine (L-Pra) has been revealed to be a natural occuring antimetabolite of methionine and leucine. Its synthetic racemate is also a powerful inhibitor of microbial growth. In search of certain enzyme inactivators. L-Pra was incorporated into dipeptides that resulted in strong suicidal substrates for microorganisms. Sinc procollagen consists mainly of the Pro-X-Gly unit which is post-translationally hydroxylated by the enzyme prolyl-4-hydroxylase (when X=Pro), we replaced X by L-Pra and studied the interaction of the resulting tripeptide with the enzyme. The synthesized peptide was characterized by NMR and mass spectrometry and its crystal structure was established by X-ray diffraction analysis.

Descriptors :   *GLYCINE, *ANTIMETABOLITES, PEPTIDES, ENZYME INHIBITORS, ANTIMICROBIAL AGENTS, COLLAGEN, NUCLEAR MAGNETIC RESONANCE, X RAY DIFFRACTION, MASS SPECTROMETRY, GERMANY.

Subject Categories : Biochemistry
      Pharmacology

Distribution Statement : APPROVED FOR PUBLIC RELEASE