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Penicillin acylase‐catalyzed protection and deprotection of amino groups as a promising approach in enzymatic peptide synthesis
Author(s) -
Didžiapetris Remigijus,
Drabnig Barbara,
Schellenberger Volker,
Jakubke Hans-Dieter,
S̆vedas Vytas
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80009-r
Subject(s) - chemistry , peptide , amino acid , enzyme , peptide synthesis , aminopeptidase , penicillin , catalysis , protease , protecting group , penicillin amidase , biochemistry , peptide bond , leucine , combinatorial chemistry , stereochemistry , organic chemistry , immobilized enzyme , antibiotics , alkyl
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.