Biochemical characterization and redesign of the coenzyme specificity of a novel monofunctional NAD+-dependent homoserine dehydrogenase from the human pathogen Neisseria gonorrhoeae
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Neisseria gonorrhoeae
Glycerol-3-phosphate dehydrogenase
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Glycerol-3-phosphate dehydrogenase
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The NADP analog and NAD diphosphate were tested for the coenzyme or inhibiting activity toward various dehydrogenases. These NAD derivatives showed little or no activity of as coenzymes for most of dehydrogenases tested. Only glyceraldehyde 3-phosphate dehydrogenase reduced the NADP analog under the high concentration of enzyme system. These NAD derivatives showed no inhibiting effect toward the reduction or oxidation of pyridine coenzymes.
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Glyceraldehyde 3-phosphate dehydrogenase
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In all organisms biomolecules play a vital role to enable proper cellular metabolism. Alteration of metabolite homoeostasis disrupts the physiology of cells, leading to various diseases [DeBerardinis and Thompson (2012) Cell, 148, 1132–1144]. Recent studies advances our understanding that some metabolites are not only involved in cellular metabolism, but also have other molecular functions. It has become evident that similar to multifunctional ‘moonlighting proteins’, ‘moonlighting metabolites’ also exists. One clear example is nicotinamide adenine dinucleotide (NAD). NAD is a ubiquitous molecule with a well-known function in many metabolic reactions, but it also has become clear that NAD is involved in the regulation of sirtuins. Sirtuins play a role in cancer, diabetes, and cardiovascular, neurodegenerative and other diseases [Donmez and Outeiro (2013) EMBO Mol. Med. 5, 344–352] and the deacetylation capacity of sirtuin proteins is NAD-dependent. This direct role of NAD in age-related diseases could not be anticipated when NAD was initially discovered as a metabolic cofactor [Donmez and Outeiro (2013) EMBO Mol. Med. 5, 344–352; Mouchiroud et al. (2013) Crit. Rev. Biochem. Mol. Biol. 48, 397–408]. Recent findings now also indicate that CoA (coenzyme A), another metabolic cofactor, can be considered as being more than ‘just’ a metabolic cofactor, and altered CoA levels lead to severe and complex effects.
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Abstract The requirements for enzymic cofactor recycling have been investigated in a system employing alcohol and lactate dehydrogenases. The interactions of various combinations of free dehydrogenases or dehydrogenases immobilized either to the same or separate supports, with free NAD, a soluble highmolecular weight derivative of NAD or an insoluble derivative of NAD have been examined.
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The content of nicotinamide coenzymes (NAD, NAD-H, NADP, NADP-H) was studied in the brain, heart and liver tissue of the newborn rats kept in hypoxic gaseous medium with a 4% oxygen content for 2 1/2 hours. There was a marked reduction of NAD content, an accumulation of NAD-H and a more than two-fold fall of the NAD/NAD-H ratio particularly marked in the brain and heart. A reduction of the NADP-H values chiefly in the liver and of the general pool of NAD-phosphates in the tissues of the newborn rats under study occurred under the same conditions. The data obtained led to the conclusion that oxygen deficiency had a significant influence on the concentration and the ratio of the nicotinamide coenzymes in the tissues of newborn rats, that in its turn led to the changes in the level and the direction of the redox processes under the conditions of hypoxia.
Hypoxia
Niacinamide
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The NADP analog and NAD diphosphate were tested for the coenzyme or inhibiting activity toward various dehydrogenases. These NAD derivatives showed little or no ac-tivity of as coenzymes for most of dehydrogenases tested. Only glyceraldehyde 3-phosphate dehydrogenase reduced the NADP analog under the high concentration of enzyme system. These NAD derivatives showed no inhibiting effect toward the reduction or oxidation of pyridine coenzymes.
Glyceraldehyde
Glyceraldehyde 3-phosphate dehydrogenase
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Hypoxia
Niacinamide
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The content of NAD+, NADH, NADP+, NADPH in the liver of normal, fasting rats, those on the low-carbohydrate diet and suffering from alloxan diabetes was studied as affected by nictotinamide. Changes in the NAD+ content, sum of nicotinamide coenzymes, the [NAD+] + [NADP+]/[NADH] +/- [NADPH] and [NAD+] + [NADH] (sum of nicotinamide coenzymes) ratios are mainly due to nicotinamide administration. Changes in the content of reduced forms of both nucleotides depend equally on nicotinamide administration and the physiological state of animals. Response of the rat organism to nicotinamide administration consists in a sharp intensification of NAD+ synthesis and in a less pronounced intensification of NADH, NADP+ and NADPH synthesis.
Niacinamide
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