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Breakdown of the stereospecificity of DD-peptidases and beta-lactamases with thiolester substrates.

Authors
  • C Damblon
  • G H Zhao
  • M Jamin
  • P Ledent
  • A Dubus
  • M Vanhove
  • X Raquet
  • L Christiaens
  • J M Frère
Publication Date
Jul 15, 1995
Source
PMC
Keywords
Disciplines
  • Biology
  • Chemistry
License
Unknown

Abstract

With peptide analogues of their natural substrates (the glycopeptide units of nascent peptidoglycan), the DD-peptidases exhibit a strict preference for D-Ala-D-Xaa C-termini. Gly is tolerated as the C-terminal residue, but with a significantly decreased activity. These enzymes were also known to hydrolyse various ester and thiolester analogues of their natural substrates. Some thiolesters with a C-terminal leaving group that exhibited L stereochemistry were significantly hydrolysed by some of the enzymes, particularly the Actinomadura R39 DD-peptidase, but the strict specificity for a D residue in the penultimate position was fully retained. These esters and thiolesters also behave as substrates for beta-lactamases. In this case, thiolesters exhibiting L stereochemistry in the ultimate position could also be hydrolysed, mainly by the class-C and class-D enzymes. However, more surprisingly, the class-C Enterobacter cloacae P99 beta-lactamase also hydrolysed thiolesters containing an L residue in the penultimate position, sometimes with a higher efficiency than the D isomer.

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