Nature of papain products resulting from inactivation by a peptidyl O‐acyl hydroxamate

FEBS Letters

Smith, Roger A.¹  Storer, Andrew C.²  Krantz, Allen¹  Robinson, Valerie J.¹  Ménard, Robert² 

[1] Syntex Research (Canada), 2100 Syntex Court, Mississauga, Ontario, Canada L5N 3X4;Biotechnology Research Institute, National Research Council of Canada, 6100 Avenue Royalmount, Montréal, Québec, Canada H4P 2R2

关键词: Cysteine protease;    Papain;    Peptidyl hydroxamate;    Oxidation;    Inhibition;    Electrospray mass spectrometry;   

DOI  :  10.1016/0014-5793(91)81376-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mass spectrometry has been used to provide insights into the mechanism of inhibition of cysteine proteases by a hydroxylamine derivative, CBZ-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.

【 授权许可】

Unknown