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Research article

S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme

David E. JENSEN, George K. BELKA, Garrett C. Du BOIS
Biochemical Journal Apr 15, 1998, 331 (2) 659-668; DOI: 10.1042/bj3310659
David E. JENSEN
Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107, U.S.A.Kimmel Cancer Institute, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107, U.S.A.Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107, U.S.A.
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  • For correspondence: djensen@hendrix.jci.tju.edu
George K. BELKA
Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107, U.S.A.Kimmel Cancer Institute, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107, U.S.A.
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Garrett C. Du BOIS
Kimmel Cancer Institute, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107, U.S.A.Department of Microbiology and Immunology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, U.S.A.
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Abstract

An enzyme isolated from rat liver cytosol (native molecular mass 78.3 kDa; polypeptide molecular mass 42.5 kDa) is capable of catalysing the NADH/NADPH-dependent degradation of S-nitrosoglutathione (GSNO). The activity utilizes 1 mol of coenzyme per mol of GSNO processed. The isolated enzyme has, as well, several characteristics that are unique to alcohol dehydrogenase (ADH) class III isoenzyme: it is capable of catalysing the NAD+-dependent oxidations of octanol (insensitive to inhibition by 4-methylpyrazole), methylcrotyl alcohol (stimulated by added pentanoate) and 12-hydroxydodecanoic acid, and also the NADH/NADPH-dependent reduction of octanal. Methanol and ethanol oxidation activity is minimal. The enzyme has formaldehyde dehydrogenase activity in that it is capable of catalysing the NAD+/NADP+-dependent oxidation of S-hydroxymethylglutathione. Treatment with the arginine-specific reagent phenylglyoxal prevents the pentanoate stimulation of methylcrotyl alcohol oxidation and markedly diminishes the enzymic activity towards octanol, 12-hydroxydodecanoic acid and S-hydroxymethylglutathione; the capacity to catalyse GSNO degradation is also checked. Additionally, limited peptide sequencing indicates 100% correspondence with known ADH class III isoenzyme sequences. Kinetic studies demonstrate that GSNO is an exceptionally active substrate for this enzyme. S-Nitroso-N-acetylpenicillamine and S-nitrosated human serum albumin are not substrates; the activity towards S-nitrosated glutathione mono- and di-ethyl esters is minimal. Product analysis suggests that glutathione sulphinamide is the major stable product of enzymic GSNO processing, with minor yields of GSSG and NH3; GSH, hydroxylamine, nitrite, nitrate and nitric oxide accumulations are minimal. Inclusion of GSH in the reaction mix decreases the yield of the supposed glutathione sulphinamide in favor of GSSG and hydroxylamine.

  • The Biochemical Society, London © 1998
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April 1998

Volume: 331 Issue: 2

Biochemical Journal: 331 (2)
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S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
David E. JENSEN, George K. BELKA, Garrett C. Du BOIS
Biochemical Journal Apr 1998, 331 (2) 659-668; DOI: 10.1042/bj3310659
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S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
David E. JENSEN, George K. BELKA, Garrett C. Du BOIS
Biochemical Journal Apr 1998, 331 (2) 659-668; DOI: 10.1042/bj3310659

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