NATURE OF PAPAIN PRODUCTS RESULTING FROM INACTIVATION BY A PEPTIDYL O-ACYL HYDROXAMATE

被引：25

作者：

MENARD, R ^{[1
]}

FENG, R ^{[1
]}

STORER, AC ^{[1
]}

ROBINSON, VJ ^{[1
]}

SMITH, RA ^{[1
]}

KRANTZ, A ^{[1
]}

机构：

[1] SYNTEX RES CANADA, MISSISSAUGA L5N 3X4, ONTARIO, CANADA

来源：

FEBS LETTERS | 1991年 / 295卷 / 1-3期

关键词：

CYSTEINE PROTEASE; PAPAIN; PEPTIDYL HYDROXAMATE; OXIDATION; INHIBITION; ELECTROSPRAY MASS SPECTROMETRY;

D O I：

10.1016/0014-5793(91)81376-J

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：

Mass spectrometry has been used to provide insights into the mechanism of inhibition of cysteine proteases by a hydroxylamine derivative. (BZ-Phe-Gly-NH-O-CO-(2,4,6-Me3)Ph. An oxidized form of papain resulting from the incubation of the enzyme with the peptidyl hydroxamate in the absence of a reducing agent has been identified as a sulfinic acid. The presence of a covalent enzyme inhibitor complex of molecular mass consistent with a sulfenamide adduct of papain could also be detected by this method. Implications on the mechanism of inactivation of cysteine proteases by peptidyl hydroxamates are discussed.

引用

页码：27 / 30

页数：4

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