S-Nitrosoglutathione as a substrate for γ-glutamyl transpeptidase

N. Hogg, Ravinder Jit Singh, Eugene Konorev, J. Joseph, B. Kalyanaraman

Research output: Contribution to journalArticle

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Abstract

S-Nitrosoglutathione (GSNO) has been used as a nitric oxide (.NO) donor compound and has also been postulated to be involved in the transport of .NO in vivo. In this study we have examined the possibility that GSNO is a substrate for γ-glutamyl transpeptidase (γ-GT), an enzyme that hydrolyses the γ-glutamyl moiety of glutathione to give glutamate and cysteinylglycine. γ-GT accelerated the decomposition of GSNO, forming S-nitrosocysteinylglycine (CG-SNO) by a mechanism inhibitable by the γ-GT inhibitors acivicin and S-methylglutathione. The K(m) of γ-GT for GSNO was found to be 28 μM. In the presence of contaminating transition metal ions, γ-GT accelerated the release of .NO from GSNO, as CG-SNO is more susceptible to transition metal ion-dependent decomposition than GSNO. However, in the presence of the transition metal ion chelator diethylenetriaminepentaacetic acid, neither GSNO nor CG-SNO decomposed to generate .NO. Neither S-methylglutathione nor acivicin affected the vasodilatory response to GSNO in an isolated perfused rat heart. However, rat kidney homogenate stimulated the decomposition of GSNO by an acivicin-inhibitable mechanism. It is likely therefore that γ-GT is involved in the decomposition of GSNO in the kidney but not in the heart.

Original languageEnglish (US)
Pages (from-to)477-481
Number of pages5
JournalBiochemical Journal
Volume323
Issue number2
StatePublished - Apr 15 1997

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acivicin
S-Nitrosoglutathione
gamma-Glutamyltransferase
Metals
Ions
Transition metals
Decomposition
Metal ions
cysteinylglycine
Substrates
Kidney
Rats
Nitric Oxide Donors
Chelating Agents
Glutathione
Glutamic Acid
Hydrolysis
Acids
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Hogg, N., Singh, R. J., Konorev, E., Joseph, J., & Kalyanaraman, B. (1997). S-Nitrosoglutathione as a substrate for γ-glutamyl transpeptidase. Biochemical Journal, 323(2), 477-481.

S-Nitrosoglutathione as a substrate for γ-glutamyl transpeptidase. / Hogg, N.; Singh, Ravinder Jit; Konorev, Eugene; Joseph, J.; Kalyanaraman, B.

In: Biochemical Journal, Vol. 323, No. 2, 15.04.1997, p. 477-481.

Research output: Contribution to journalArticle

Hogg, N, Singh, RJ, Konorev, E, Joseph, J & Kalyanaraman, B 1997, 'S-Nitrosoglutathione as a substrate for γ-glutamyl transpeptidase', Biochemical Journal, vol. 323, no. 2, pp. 477-481.
Hogg N, Singh RJ, Konorev E, Joseph J, Kalyanaraman B. S-Nitrosoglutathione as a substrate for γ-glutamyl transpeptidase. Biochemical Journal. 1997 Apr 15;323(2):477-481.
Hogg, N. ; Singh, Ravinder Jit ; Konorev, Eugene ; Joseph, J. ; Kalyanaraman, B. / S-Nitrosoglutathione as a substrate for γ-glutamyl transpeptidase. In: Biochemical Journal. 1997 ; Vol. 323, No. 2. pp. 477-481.
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