The use of penicillin acylase for selective N-terminal deprotection in peptide synthesis

✍ Scribed by Herbert Waldmann

• Book ID: 104220173
• Publisher: Elsevier Science
• Year: 1988
• Tongue: French
• Weight: 229 KB
• Volume: 29
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(00)86668-x

✦ Synopsis

Penicillin acylase from E. coli (EC 351.11) accepts a broad range of Nphenylacetyl-dipeptide esters as substrates. The enzyme hydrolyses the N-terminal protecting group selectively at room temp. and pH=8.1 without affecting the peptide-or the ester-bonds. Alternatively methyl-, benzyl-, tert-butyl and ally1 esters can be cleaved chemically leaving the phenylacetamido moiety intact.