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Enzimatic Synthesis of Aspartyl-containing Dipeptides by Laurence Adisson; Jean Bolte; Colette Demuynck; Jean-Claude Mani is a Chemistry article available to read on EtoBox.

What is Enzimatic Synthesis of Aspartyl-containing Dipeptides about?

We show that ths ability of thermlysin to catalyze the coupling of aspartyl residus with other minoacids is restricted to ptmnylalanine. Ezsterification of the two carboxylic grcups of N-protected aspartic acid allows chymotrypsin and papain to catalyze the desired synthssis. Ths uss of proteases to catalyze peptide bad formation is an interesting alternative to chemical msthcds. lhs main advantage is to avoid the risk of racemizaticn, and, althargh yields are not always excellent, many studies ha\Fe been reported in the last few yearsl. AccotXliq to the nature of enzymes and substrates, the syntheses will run under thermodynamic or kinetic control. In ths four case, the psptide bond is formed by ttm reverss prazess of ths hydrolysis (schfm I) : the problem is to displace the equilibriun tcxmrds synthesis. In ths second cass (scheme II), for serine and thiol proteases, the "acyl donor" substrate is an ester, ths covalent acyl-enzyme intermdiate is deacylated Ttitively by water and ths ?ucleophilic" amimacids. It is then possible to obtain a high cmcentraticm of peptide, after a short tims, then ths reaction can go back and reach ths equilibriun position lb,\*,3 .

Who reads Enzimatic Synthesis of Aspartyl-containing Dipeptides?

Author

Laurence Adisson; Jean Bolte; Colette Demuynck; Jean-Claude Mani

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0040-4020)

Published

1988

Language

EN

Field

Chemistry (Physical Sciences)