INHIBITION OF PAPAIN BY PEPTIDE NITRILES - REACTIONS OF EXTERNAL NUCLEOPHILES WITH THE THIOIMIDATE ESTER ADDUCT

被引：10

作者：

GOURSALIN, BJ ^{[1
]}

STORER, AC ^{[1
]}

CASTELHANO, A ^{[1
]}

KRANTZ, A ^{[1
]}

ROBINSON, V ^{[1
]}

机构：

[1] SYNTEX,MISSISSAUGA,ONTARIO,CANADA

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1991年 / 13卷 / 05期

关键词：

PAPAIN; N-(N-ACETYL-L-PHENYLALANYL)GLYCINENITRILE; N-(N-ACETYL-L-PHENYLALANYL)GLYCINAMIDE; ENZYME INHIBITOR; C-13-NMR; N-15-NMR;

D O I：

10.1016/0141-0229(91)90203-M

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

N-(N-Acetyl-L-phenylalanyl)glycinenitrile is a reversible inhibitor of papain which forms a thioimidate adduct with the cysteine thiol in the enzyme's active site. It is possible for this thioimidate to undergo reactions with external thiols, namely beta-mercaptoethanol and N-acetylcysteamine. The reactions were followed by C-13- and N-15-NMR techniques which indicated that the initial nitrile was converted to N-(N-acetyl-L-phenylalanyl)glycinamide and then further hydrolysed to N-(N-acetyl-L-phenylalanyl)glycine. In essence papain is acting as a nitrile hydratase, and this activity, coupled with papain's well-characterized amidase activity, results in the synthesis of a carboxylic acid from a nitrile.

引用

页码：408 / 411

页数：4

共 21 条

[1]

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[2] PAPAIN CATALYZED PEPTIDE-SYNTHESIS - CONTROL OF AMIDASE ACTIVITY AND THE INTRODUCTION OF UNUSUAL AMINO-ACIDS [J].