Cellular NAD(P)H-dependent oxidoreductase activity with artificial dyes (NAD(P)H-OR) is an indicator of viability, as the cellular redox state is important for biosynthesis and antioxidant defense. However, high NAD(P)H due to impaired mitochondrial oxidation, known as reductive stress, should increase NAD(P)H-OR yet perturb viability. To better understand this complex behavior, we assayed NAD(...

Several microorganisms can utilize l-rhamnose as a carbon and energy source through the nonphosphorylative metabolic pathway, in which 1-dehydrogenase (RhaDH) catalyzes NAD(P)+-dependent oxidization of to l-rhamnono-1,4-lactone. We herein investigated crystal structures RhaDH from Azotobacter vinelandii ligand-free, NAD+-bound, NADP+-bound, l-rhamnose- NAD+-bound forms at 1.9, 2.1, 2.4, 1.6 Å r...

NAD is an essential metabolite that exists in NAD(+) or NADH form in all living cells. Despite its critical roles in regulating mitochondrial energy production through the NAD(+)/NADH redox state and modulating cellular signaling processes through the activity of the NAD(+)-dependent enzymes, the method for quantifying intracellular NAD contents and redox state is limited to a few in vitro or e...

background: phenylalanine dehydrogenase (phedh ec 1.4.1.20) is a nad+-dependent enzyme that performs the reversible oxidative deamination of l-phenylalanine to phenylpyruvate. it plays an important role in detection and screening of phenylketonuria (pku) diseases and production of chiral intermediates as well. the main goal of this study was to find a simple and rapid alternative method for pur...

The in vivo regulation of glutamate dehydrogenase (GDH) was studied in Mucor racemosus as a function of nutritional conditions and morphological state. Both nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP)-dependent GDH activities were found. The effect of carbon and nitrogen source on the specific activity of the NAD-dependent GDH suggests that its...

Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both ...

NAD+ is an essential co-enzyme for redox reactions and is consumed in lysine deacetylation and poly(ADP-ribosyl)ation. NAD+ synthetase catalyzes the final step in NAD+ synthesis in the well characterized de novo, salvage, and import pathways. It has been long known that eukaryotic NAD+ synthetases use glutamine to amidate nicotinic acid adenine dinucleotide while many purified prokaryotic NAD+ ...

Nicotinamide Adenine Dinucleotide (NAD⁺) is known mainly as coenzyme of redox reactions for energy transduction and is consumed as substrate in regulatory reactions removing nicotinamide and producing ADP-ribose. Several families of ADP-ribose synthesizing enzymes use NAD⁺ as substrate and control processes like DNA repair, replication and transcription, chromatin structure, the activity of G-p...