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Published online before print September 30, 2005, 10.1110/ps.051641005
Protein Science (2005), 14:2922-2928. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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FOR THE RECORD

Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase

Noureddine Rhazi1, Michael Delmarcelle1, Eric Sauvage1, Françoise Jacquemotte2, Kris Devriendt3, Valérie Tallon4,5, Léon Ghosez4,5 and Jean-Marie Frère1

1 Centre d’Ingénierie de Protéines, Universitéde Liège, Institut de Chimie B6, Sart-Tilman, B-4000 Liège, Belgium
2 Département des Substances Naturelles et Biochimie, Institut Meurice, Haute Ecole Lucia de Brouckère, B-1070 Bruxelles, Belgium
3 Laboratorium voor Eiwitbiochemie and Eiwitengineering, Universiteit Gent, B-9000 Gent, Belgium
4 ORSY, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium

(RECEIVED June 9, 2005; FINAL REVISION July 5, 2005; ACCEPTED July 11, 2005)

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.

Keywords: D-Ala-D-Ala peptidase; transpeptidation; reversibility; specificity; {beta}-lactam antibiotic; penicillin binding protein; enzymes; active sites; thermodynamics; hydrodynamics; kinetics; mechanism

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051641005.

Reprint requests to: Jean-Marie Frère, Centre d’Ingénierie de Protéines, Universitéde Liège, Institut de Chimie B6, Sart-Tilman, B-4000 Liège, Belgium; e-mail: jmfrere{at}ulg.ac.be; fax: +32-4-3663364.


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