Penicillin acylase-catalyzed protection and deprotection of amino groups as a promising approach in enzymatic peptide synthesis

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 enzym...

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Bibliographic Details
Published in:	FEBS letters Vol. 287; no. 1; pp. 31 - 33
Main Authors:	Didžiapetris, Remigijus, Drabnig, Barbara, Schellenberger, Volker, Jakubke, Hans-Dieter, S̆vedas, Vytas
Format:	Journal Article
Language:	English
Published:	Amsterdam Elsevier B.V 05-08-1991 Elsevier
Subjects:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Enkephalin, Leucine - biosynthesis Enkephalin, Leucine - chemistry Enzymatic peptide synthesis. Enzymatic amino group protection and deprotection: Papain Enzymes and enzyme inhibitors Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Hydrolases Kinetics Leucineenkephalin methyl ester Molecular Sequence Data OBut OMe papain Papain - metabolism penicillin acylase Penicillin acylase ( E. coli) Penicillin Amidase - metabolism PhAc Phenylacetates - metabolism phenylacetyl t-butyl ester α-Chymotrypsin α-Chymotrypsin P Penicillin acylase ( E. coli) CT PA Enzymatic peptide synthesis. Enzymatic amino group protection and deprotection: Papain OMe Leucineenkephalin OBu t PhAc Enzymatic synthesis Enzyme Escherichia coli Enkephalin Chemical protection Bacteria Peptide synthesis N terminal peptide Enterobacteriaceae Penicillin V acylase
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(91)80009-R