Cys25-nitrosylation inactivates papain

Giorgio Venturini, Emanuela Fioravanti, Marco Colasanti, Tiziana Persichini, Paolo Ascenzi

Research output: Contribution to journalArticle

19 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)425-428
Number of pages4
JournalBiochemistry and Molecular Biology International
Volume46
Issue number2
Publication statusPublished - 1998

Fingerprint

Papain
Nitric Oxide
Cysteine Proteases
Molecular Models
Nitric Oxide Donors
Nitroprusside
Catalyst activity

Keywords

  • Cys25-nitrosylation
  • Enzyme inhibition
  • Papain

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

Cite this

Venturini, G., Fioravanti, E., Colasanti, M., Persichini, T., & Ascenzi, P. (1998). Cys25-nitrosylation inactivates papain. Biochemistry and Molecular Biology International, 46(2), 425-428.

Cys25-nitrosylation inactivates papain. / Venturini, Giorgio; Fioravanti, Emanuela; Colasanti, Marco; Persichini, Tiziana; Ascenzi, Paolo.

In: Biochemistry and Molecular Biology International, Vol. 46, No. 2, 1998, p. 425-428.

Research output: Contribution to journalArticle

Venturini, G, Fioravanti, E, Colasanti, M, Persichini, T & Ascenzi, P 1998, 'Cys25-nitrosylation inactivates papain', Biochemistry and Molecular Biology International, vol. 46, no. 2, pp. 425-428.
Venturini G, Fioravanti E, Colasanti M, Persichini T, Ascenzi P. Cys25-nitrosylation inactivates papain. Biochemistry and Molecular Biology International. 1998;46(2):425-428.
Venturini, Giorgio ; Fioravanti, Emanuela ; Colasanti, Marco ; Persichini, Tiziana ; Ascenzi, Paolo. / Cys25-nitrosylation inactivates papain. In: Biochemistry and Molecular Biology International. 1998 ; Vol. 46, No. 2. pp. 425-428.
@article{b4de73a2c0c84326a21a2e1e0b31866f,
title = "Cys25-nitrosylation inactivates papain",
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.",
keywords = "Cys25-nitrosylation, Enzyme inhibition, Papain",
author = "Giorgio Venturini and Emanuela Fioravanti and Marco Colasanti and Tiziana Persichini and Paolo Ascenzi",
year = "1998",
language = "English",
volume = "46",
pages = "425--428",
journal = "Biochemistry and Molecular Biology International",
issn = "1039-9712",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Cys25-nitrosylation inactivates papain

AU - Venturini, Giorgio

AU - Fioravanti, Emanuela

AU - Colasanti, Marco

AU - Persichini, Tiziana

AU - Ascenzi, Paolo

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

KW - Cys25-nitrosylation

KW - Enzyme inhibition

KW - Papain

UR - http://www.scopus.com/inward/record.url?scp=0031767133&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031767133&partnerID=8YFLogxK

M3 - Article

C2 - 9801811

AN - SCOPUS:0031767133

VL - 46

SP - 425

EP - 428

JO - Biochemistry and Molecular Biology International

JF - Biochemistry and Molecular Biology International

SN - 1039-9712

IS - 2

ER -