PENICILLIN ACYLASE-CATALYZED PROTECTION AND DEPROTECTION OF AMINO-GROUPS AS A PROMISING APPROACH IN ENZYMATIC PEPTIDE-SYNTHESIS

被引:29
作者
DIDZIAPETRIS, R
DRABNIG, B
SCHELLENBERGER, V
JAKUBKE, HD
SVEDAS, V
机构
[1] AN BELOZERSKII MOLEC BIOL & BIOORGAN CHEM LAB,MOSCOW 119899,USSR
[2] KARL MARX UNIV,DEPT BIOCHEM,DIV BIOSCI,O-7010 LEIPZIG,GERMANY
关键词
PENICILLIN ACYLASE (ESCHERICHIA-COLI); ENZYMATIC PEPTIDE SYNTHESIS; ENZYMATIC AMINO GROUP PROTECTION AND DEPROTECTION; PAPAIN; ALPHA-CHYMOTRYPSIN; LEUCINE-ENKEPHALIN;
D O I
10.1016/0014-5793(91)80009-R
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
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页码:31 / 33
页数:3
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