Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase
(2005) Protein Science — Vol. 14, n° 11, p. 2922-2928 (2005)
Files
No attached file found for this publication.
Details
- Authors
- Abstract
- The specificity of the Streptomyces R61 penicillin-sensitive D-Ala-D-Ala peptidase has been re-examined with the help of synthetic substrates. The products of the transpeptidation reactions obtained with Gly-L-Xaa dipeptides as acceptor substrates are themselves poor substrates of the enzyme. This is in apparent contradiction with the classically accepted specificity rules for D-Ala-D-Ala peptidases. The Gly-L-Xaa dipeptide is regenerated by both the hydrolysis and transpeptidation reactions. The latter reaction is observed when another Gly-L-Xaa peptide or D-Alanine are supplied as acceptors. Utilization of substrates in which the terminal -COO- group has been esterified or amidated shows that a free carboxylate is not an absolute prerequisite for activity. The results are discussed in the context of the expected reversibilty of the transpeptidation reaction.
- Affiliations
Citations
Rhazi, N., Delmarcelle, M., Sauvage, E., Jacquemotte, F., Devriendt, K., Tallon, V., Ghosez, L., & Frère, J.-M. (2005). Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase. Protein Science, 14(11), 2922-2928. https://doi.org/10.1110/ps.051641005 (Original work published 2005)