Cys25-nitrosylation inactivates papain

G Venturini; E Fioravanti; M Colasanti; T Persichini; P Ascenzi

doi:10.1080/15216549800203942

Cys25-nitrosylation inactivates papain

Biochem Mol Biol Int. 1998 Oct;46(2):425-8. doi: 10.1080/15216549800203942.

Authors

G Venturini¹, E Fioravanti, M Colasanti, T Persichini, P Ascenzi

Affiliation

¹ Department of Biology, University of Rome Tre, Italy.

PMID: 9801811
DOI: 10.1080/15216549800203942

Abstract

Nitric oxide (NO) may modulate the catalytic activity of cysteine proteases. In the present study, the inhibitory effect of NO, released by the NO-donors (+/-)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide and nitroprusside, on papain action is reported. Papain inactivation via NO-mediated nitrosylation of the Cys25 catalytic residue represents a molecular model for cysteine protease inhibition.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cysteine / metabolism*
Cysteine Proteinase Inhibitors / pharmacology*
Nitric Oxide / metabolism
Nitric Oxide / pharmacology*
Nitro Compounds / pharmacology
Nitroprusside / pharmacology
Papain / antagonists & inhibitors*
Papain / metabolism*

Substances

Cysteine Proteinase Inhibitors
Nitro Compounds
Nitroprusside
Nitric Oxide
FK 409
Papain
Cysteine