Synthesis of amino-acid derivatives and dipeptides with an original peptidase enzyme.
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.
Auriol
D
D
BioEurope, Toulouse, France.
Paul
F
F
Yoshpe
I
I
Gripon
J C
JC
Monsan
P
P
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
D000596:Amino Acids; D004151:Dipeptides; D010450:Endopeptidases; D001218:Aspartame