Escherichia coli DNA ligase (LigA) is the prototype of the NAD(+)-dependent class of DNA ligases found in all bacteria. Here we report the characterization of E.coli LigB, a second NAD(+)-dependent DNA ligase identified by virtue of its sequence similarity to LigA. LigB differs from LigA in that it lacks the BRCA1 C-terminus domain (BRCT) and two of the four Zn-binding cysteines that are presen...

The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 A and 2.4 A resolutions. The structures reveal tha...

interaction of glucose 6-phosphate dehydrogenase from s. aureofaciens with nad+, nadp+and glucose 6-phosphate were investigated using different fluorescent probes. binding of nad+, nadp+and s-nadph to the native enzyme quenched intrinsic protein fluorescence by 100%, 10% and 21%,respectively, from which kd values of nad+ (6.5 mm), nadp+ (92.0 μm) and s-nadph (122.0 μm)were calculated. binding o...

E. coli flavohemoglobin, oriented at electrodes via amphiphilic polymyxin B, electrocatalytically interconverts NADH and NAD(+) at its heme potentials operating as an electron transfer relay between the electrode and the protein FAD, where NADH/NAD(+) is transformed. The results are crucial for the development of NAD(+)-dependent bioelectrodes for biosynthesis, biosensors and biofuel cells.

Electrochemical enzymatic biosensors represent a promising, low-cost technology for point-of-care (POC) diagnostics that allows fast response and simple sample processing procedures. In this review, we summarize up-to-date literature on NAD+/NADH (β-nicotinamide adenine dinucleotide)-dependent electrochemical dehydrogenase highlight their applications in human physiological fluids. A brief comp...

Background NAMPT (Nicotinamide phosphoribosyltransferase) catalyzes the rate-limiting step in the NAD-biosynthesis from nicotinamide and regulates the activity of NADdependent enzymes. Cancer cells are highly dependent on NAD for energy and DNA repair processes and are expected to be more susceptible to the inhibition of NAD synthesis than non-transformed cells. Can inhibition of NAMPT by FK866...

Familial forms of Parkinson's disease (PD) caused by mutations in PINK1 are linked to mitochondrial impairment. Defective mitochondria are also found in Drosophila models of PD with pink1 mutations. The co-enzyme nicotinamide adenine dinucleotide (NAD+) is essential for both generating energy in mitochondria and nuclear DNA repair through NAD+-consuming poly(ADP-ribose) polymerases (PARPs). We ...

It is generally known that cofactors play a major role in the production of different fermentation products. This paper is part of a systematic study that investigates the potential of cofactor manipulations as a new tool for metabolic engineering. The NADH/NAD+ cofactor pair plays a major role in microbial catabolism, in which a carbon source, such as glucose, is oxidized using NAD+ and produc...

Nicotinamide adenine dinucleotide (NAD+) is an established cofactor for enzymes serving cellular metabolic reactions. More recent research identified NAD+ as a signaling molecule and substrate for sirtuins and poly-adenosine 5'-diphosphate polymerases; enzymes that regulate protein deacetylation and DNA repair, and translate changes in energy status into metabolic adaptations. Deranged NAD+ hom...

amino acid dehydrogenases (l-amino acid: oxidoreductase deaminating ec 1.4.1.x) are members of the wider superfamily of oxidoreductases that catalyze the reversible oxidative deamination of an amino acid to its keto acid and ammonia with the concomitant reduction of either nad+, nadp+ or fad. these enzymes have been received much attention as biocatalysts for use in biosensors or diagnostic kit...