title: Synthesis of amino-acid derivatives and dipeptides with an original peptidase enzyme.
abstract: 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.
authors.affiliation: BioEurope, Toulouse, France.
authors.forename: D
authors.initials: D
authors.lastname: Auriol
authors.forename: F
authors.initials: F
authors.lastname: Paul
authors.forename: I
authors.initials: I
authors.lastname: Yoshpe
authors.forename: J C
authors.initials: JC
authors.lastname: Gripon
authors.forename: P
authors.initials: P
authors.lastname: Monsan
mesh_terms: D000596:Amino Acids / Q000138:chemical synthesis* / Q000737:chemistry; D001218:Aspartame / Q000138:chemical synthesis; D004151:Dipeptides / Q000138:chemical synthesis* / Q000737:chemistry; D010450:Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D013210:Staphylococcus / Q000201:enzymology
chemical_list: D000596:Amino Acids; D004151:Dipeptides; D010450:Endopeptidases; D001218:Aspartame