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Synthesis of amino-acid derivatives and dipeptides with an original peptidase enzyme

Auriol, D.; Paul, F.; Yoshpe, I.; Gripon, J.C.; Monsan, P.

Biomedica Biochimica Acta 50(10-11): S163-S168

1991

ISSN/ISBN: 0232-766X
PMID: 1820040
Document Number: 387046
A peptidase from the non pathogenic Staphylococcus sp. strain BEC 299 was purified to a final specific activity of 84,400 U/mg protein. Its molecular weight is 450 kDa and optimum pH 10.0. This enzyme catalyzes the synthesis of dipeptides (aspartame) and alpha-amino acid derivatives (N-L-malyl-L-tyrosine ethyl ester). The influence of cosolvents and pH on dipeptides and alpha-amino acid derivative synthesis is described. Finally, we detail the use of the peptidase as a reagent in protease-catalyzed peptide synthesis.

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