S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
| Autor: | D E Jensen, G K Belka, G C Du Bois |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Octanols
Phenylglyoxal Stereochemistry Molecular Sequence Data Biochemistry Formaldehyde dehydrogenase activity Substrate Specificity S-Nitrosoglutathione chemistry.chemical_compound Cytosol Hydroxylamine Animals Amino Acid Sequence Molecular Biology Alcohol dehydrogenase Ethanol biology Chemistry Alcohol Dehydrogenase Lauric Acids Cell Biology Glutathione NAD Rats Isoenzymes Kinetics Liver biology.protein NAD+ kinase Nitroso Compounds Research Article |
| Zdroj: | Biochemical Journal. 331:659-668 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3310659 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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