The Phenylacetyl (PhAc) Group as Enzymatically Removable Protecting Function for Peptides and Carbohydrates: Selective Deprotections with Penicillin Acylase
Using the modified carbodiimide procedure or EEDQ as coupling reagent, N-Phenylacetyl (PhAc) amino acids are condensed in good yields with amino acid methyl, benzyl, allyl, and tert-butyl esters to give totally protected dipeptides.The PhAc group is stabl
Waldmann, Herbert
p. 1175 - 1180
(2007/10/02)
THE USE OF PENICILLIN ACYLASE FOR SELECTIVE N-TERMINAL DEPROTECTION IN PEPTIDE SYNTHESIS
Penicillin acylase from E. coli (EC 3.5.1.11) accepts a broad range of N-phenylacetyl-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 allyl esters can be cleaved chemically leaving the phenylacetamido moiety intact.
Waldmann, Herbert
p. 1131 - 1134
(2007/10/02)
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