CONVERSION OF ACTIVE-SITE CYSTEINE RESIDUE OF PAPAIN INTO A DEHYDRO-SERINE, A SERINE AND A GLYCINE RESIDUE

被引：32

作者：

CLARK, PI ^{[1
]}

LOWE, G ^{[1
]}

机构：

[1] UNIV OXFORD,DYSON PERRINS LAB,OXFORD OX1 3QY,ENGLAND

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1978年 / 84卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1978.tb12168.x

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：

Photolysis of papain which had been inhibited with 2‐bromo‐2′,4′‐dimethoxyacetophenone regenerated papain, but also formed [δSer25]papain (i.e. papain in which the active‐site cysteine residue 25 was replaced by dehydroserine) via the intermediate dehydrocysteine analogue, [δCys25]‐papain. Reduction with sodium borohydride gave [Ser25]papain. Both [Ser25]papain and [δSer25]‐papain had binding properties similar to those of papain, but were devoid of enzymic activity. Their fluorescence properties were also investigated. Incubation of [δSer25]papain at pH 9.0 gave [Gly25]papain. Copyright © 1978, Wiley Blackwell. All rights reserved

引用

页码：293 / 299

页数：7

共 37 条

[11]

Drenth J, 1971, ENZYMES, V3, P485

[12] FORMATION OF STABLE CRYSTALLINE ENZYME-SUBSTRATE INTERMEDIATES AT SUB-ZERO TEMPERATURES [J].