title: Penicillin acylase-catalyzed protection and deprotection of amino groups as a promising approach in enzymatic peptide synthesis.
abstract: Penicillin acylase from E. coli is able to catalyze both the introduction and the removal of the phenylacetyl group. We have established that phenylacetyl derivatives of amino acids and peptides can be used in protease-catalyzed peptide synthesis. Here the synthesis of leucine-enkephalin using enzymes for N-terminal amino group protection, peptide bond formation and deprotection is described.
authors.affiliation: A.N. Belozersky Institute of Physio-Chemical Biology, Moscow State University, USSR.
authors.forename: R
authors.initials: R
authors.lastname: Didziapetris
authors.forename: B
authors.initials: B
authors.lastname: Drabnig
authors.forename: V
authors.initials: V
authors.lastname: Schellenberger
authors.forename: H D
authors.initials: HD
authors.lastname: Jakubke
authors.forename: V
authors.initials: V
authors.lastname: Svedas
mesh_terms: D000595:Amino Acid Sequence; D004743:Enkephalin, Leucine / Q000096:biosynthesis* / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008969:Molecular Sequence Data; D010206:Papain / Q000378:metabolism; D010399:Penicillin Amidase / Q000378:metabolism*; D010648:Phenylacetates / Q000378:metabolism
chemical_list: D010648:Phenylacetates; D004743:Enkephalin, Leucine; D010206:Papain; D010399:Penicillin Amidase; C025136:phenylacetic acid