Search results for "Branched-chain alpha-keto acid dehydrogenase complex"
showing 4 items of 4 documents
Influence of carboxylic acids on the stereospecific nicotinamide adenine dinucleotide-dependent and nicotinamide adenine dinucleotide-independent lac…
1971
Leuconostoc mesenteroides increased its lactic acid production from glucose threefold when malic acid was added to the culture. This increase resulted also in a reduction of the ratio of d -lactic acid to l -lactic acid (31.5 to 1.23). Addition of malic acid increased 6.5-fold the specific activity of nicotinamide adenine dinucleotide (NAD)-linked l -lactate dehydrogenase and increased 3.2-fold that of NAD-linked d -lactate dehydrogenase. The Michaelis constant ( K m ) for NAD of the NAD-linked l -lactate dehydrogenase increased with the addition of malate, but no change was observed in the K m values for the respective d -enzyme. The effect of carboxylic acids on the NAD-linked l -lactate…
Role of Reduced Lipoic Acid in the Redox Regulation of Mitochondrial Aldehyde Dehydrogenase (ALDH-2) Activity
2007
Chronic therapy with nitroglycerin results in a rapid development of nitrate tolerance, which is associated with an increased production of reactive oxygen species. We have recently shown that mitochondria are an important source of nitroglycerin-induced oxidants and that the nitroglycerin-bioactivating mitochondrial aldehyde dehydrogenase is oxidatively inactivated in the setting of tolerance. Here we investigated the effect of various oxidants on aldehyde dehydrogenase activity and its restoration by dihydrolipoic acid. In vivo tolerance in Wistar rats was induced by infusion of nitroglycerin (6.6 microg/kg/min, 4 days). Vascular reactivity was measured by isometric tension studies of iso…
Interaction of the mitochondrial membrane D-3-hydroxybutyrate dehydrogenase with fluorescent phospholipids
1993
Norbert Latruffe l ,I, Boubker Nasser ‘, Claude Morpain 3, Jiirgen Zirkel 4, Michael Seiter 4, Bernard Laude 3 and Wolfgang Trommer 4 ’ Laboratoire de Biobgie Mol&laire et Cellulaire, Universite’ de Bourgogne, Fact& des Sciences Mirande, BP 138, 21004 D@on Cedex (France) 2 Laboratoire de Biochimie &A CNRS 531) and 3 Laboratoire de Chimie Organique, Universite’ de Franche-Comte 25030 Besaqon Cedex (France) 4 Fachbereich Chemie, Universitiit Kaiserslautem, D 6750 Kaiserslautem (Germany)
Nitrate Reductase Activity of Mitochondrial Aldehyde Dehydrogenase (ALDH-2) as a Redox Sensor for Cardiovascular Oxidative Stress
2009
In 2002, mitochondrial aldehyde dehydrogenase (ALDH-2) was identified as an organic nitrate bioactivating enzyme. This so-called nitrate reductase activity denitrates nitroglycerin (glycerol trinitrate) to its 1,2-glycerol dinitrate metabolite and nitrite. This reaction relies on reduced thiols at the active site of the enzyme and on the presence of reduced dithiols as the electron source. During bioconversion of nitroglycerin, and also in the presence of reactive oxygen and nitrogen species, the active site thiols of ALDH-2 are oxidized and the enzyme looses its activity. We, therefore, speculated that ALDH-2 activity could be a useful marker for cardiovascular oxidative stress. Indeed, th…