Synonyms containing nad nucleosidase

We've found 190 synonyms:

Nicotinamide adenine dinucleotide

Nicotinamide adenine dinucleotide

Nicotinamide adenine dinucleotide, abbreviated NAD+, is a coenzyme found in all living cells. The compound is a dinucleotide, since it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine base and the other nicotinamide. In metabolism, NAD+ is involved in redox reactions, carrying electrons from one reaction to another. The coenzyme is, therefore, found in two forms in cells: NAD+ is an oxidizing agent – it accepts electrons from other molecules and becomes reduced. This reaction forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the main function of NAD+. However, it is also used in other cellular processes, the most notable one being a substrate of enzymes that add or remove chemical groups from proteins, in posttranslational modifications. Because of the importance of these functions, the enzymes involved in NAD+ metabolism are targets for drug discovery. In organisms, NAD+ can be synthesized from simple building-blocks from the amino acids tryptophan or aspartic acid. In an alternative fashion, more complex components of the coenzymes are taken up from food as the vitamin called niacin. Similar compounds are released by reactions that break down the structure of NAD+. These preformed components then pass through a salvage pathway that recycles them back into the active form. Some NAD+ is also converted into nicotinamide adenine dinucleotide phosphate; the chemistry of this related coenzyme is similar to that of NAD+, but it has different roles in metabolism.

— Freebase

Niacin

Niacin

Niacin is an organic compound with the formula C 6H 5NO 2 and, depending on the definition used, one of the 40 to 80 essential human nutrients. Niacin is one of five vitamins associated with a pandemic deficiency disease: niacin deficiency, vitamin C deficiency, thiamin deficiency, vitamin D deficiency, vitamin A deficiency. Niacin has been used for over 50 years to increase levels of HDL in the blood and has been found to modestly decrease the risk of cardiovascular events in a number of controlled human trials. This colorless, water-soluble solid is a derivative of pyridine, with a carboxyl group at the 3-position. Other forms of vitamin B3 include the corresponding amide, nicotinamide, where the carboxyl group has been replaced by a carboxamide group, as well as more complex amides and a variety of esters. Nicotinic acid and niacinamide are convertible to each other with steady world demand rising from 8500 tonnes per year in 1980s to 40,000 in recent years. Niacin cannot be directly converted to nicotinamide, but both compounds could be converted to NAD and NADP in vivo. Nicotinic acid, nicotinamid, and tryptophan are co-factors for nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate. NAD converts to NADP by phosphorylation in the presence of the enzyme NAD+ kinase. NADP and NAD are coenzyme for many dehydrogenases, participating in many hydrogen transfer processes. NAD is important in catabolism of fat, carbohydrate, protein and alcohol as well as cell signaling and DNA repair and NADP mostly in anabolism reaction such as fatty acid and cholesterol synthesis. High energy requirements or high turnover rate organs are usually the most susceptible to their deficiency. Although the two are identical in their vitamin activity, nicotinamide does not have the same pharmacological effects as niacin. Nicotinamide does not reduce cholesterol or cause flushing. Nicotinamide may be toxic to the liver at doses exceeding 3 g/day for adults. Niacin is a precursor to NAD+/NADH and NADP+/NADPH, which play essential metabolic roles in living cells. Niacin is involved in both DNA repair, and the production of steroid hormones in the adrenal gland.

— Freebase

NADH

NADH

nicotinamide adenine dinucleotide (NAD) carrying two electrons and bonded with a hydrogen (H) ion; the reduced form of NAD.

— Wiktionary

na

na

.na is the Internet country code top-level domain for Namibia. Registry/Registrar Separation has been implemented, with Namibian and Foreign Registrars being accredited. The Registry supports a Web/GUI interface and EPP. Registrations are available at the second level or at the third level beneath various names that include some redundant choices. Prices vary depending on the level at which a registration is made, the second-level name a third-level registration is beneath, and whether the registrant is domestic or foreign. .na domains cost approximately 4000 NAD a year for domestic and 40000 NAD for foreign registrants, .com.na 400 and 4000 NAD respectively, and .co.na 500 NAD for both. NA-NiC is a member of CoCCA and uses their Dispute Resolution.

— Freebase

Leucine dehydrogenase

Leucine dehydrogenase

In enzymology, a leucine dehydrogenase is an enzyme that catalyzes the chemical reaction++ The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-leucine:NAD+ oxidoreductase. Other names in common use include L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, and LeuDH. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis.

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Fructuronate reductase

Fructuronate reductase

In enzymology, a fructuronate reductase is an enzyme that catalyzes the chemical reaction++ Thus, the two substrates of this enzyme are D-mannonate and NAD+, whereas its 3 products are D-fructuronate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-mannonate:NAD+ 5-oxidoreductase. Other names in common use include mannonate oxidoreductase, mannonic dehydrogenase, D-mannonate dehydrogenase, and D-mannonate:NAD+ oxidoreductase. This enzyme participates in pentose and glucuronate interconversions.

— Freebase

Homoserine dehydrogenase

Homoserine dehydrogenase

In enzymology, a homoserine dehydrogenase is an enzyme that catalyzes the chemical reaction++ The 2 substrates of this enzyme are L-homoserine and NAD+, whereas its 3 products are L-aspartate 4-semialdehyde, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-homoserine:NAD+ oxidoreductase. Other names in common use include HSDH, and HSD. Homoserine dehydrogenase catalyses the third step in the aspartate pathway; the NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. Homoserine is an intermediate in the biosynthesis of threonine, isoleucine, and methionine.

— Freebase

Sirtuin

Sirtuin

Sirtuin or Sir2 proteins are a class of proteins that possess either mono-ribosyltransferase, or deacylase activity, including deacetylase, desuccinylase, demalonylase, demyristoylase and depalmitoylase activity. Sirtuins regulate important biological pathways in bacteria, archaea and eukaryotes. The name Sir2 comes from the yeast gene 'silent mating-type information regulation 2', the gene responsible for cellular regulation in yeast. Sirtuins have been implicated in influencing a wide range of cellular processes like aging, transcription, apoptosis, inflammation and stress resistance, as well as energy efficiency and alertness during low-calorie situations. Sirtuins can also control circadian clocks and mitochondrial biogenesis. Yeast Sir2 and some, but not all, sirtuins are protein deacetylases. Unlike other known protein deacetylases, which simply hydrolyze acetyl-lysine residues, the sirtuin-mediated deacetylation reaction couples lysine deacetylation to NAD hydrolysis. This hydrolysis yields O-acetyl-ADP-ribose, the deacetylated substrate and nicotinamide, itself an inhibitor of sirtuin activity. The dependence of sirtuins on NAD links their enzymatic activity directly to the energy status of the cell via the cellular NAD:NADH ratio, the absolute levels of NAD, NADH or nicotinamide or a combination of these variables.

— Freebase

Dihydrodipicolinate reductase

Dihydrodipicolinate reductase

In enzymology, a dihydrodipicolinate reductase is an enzyme that catalyzes the chemical reaction+ The 3 substrates of this enzyme are-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, NAD+, and NADP+, whereas its 4 products are 2,3-dihydrodipicolinate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD+ oxidoreductase. Other names in common use include dihydrodipicolinic acid reductase, and 2,3,4,5-tetrahydrodipicolinate:NAD+ oxidoreductase. This enzyme participates in lysine biosynthesis.

— Freebase

Alanine dehydrogenase

Alanine dehydrogenase

Alanine dehydrogenase is an enzyme that catalyzes the chemical reaction++ The 3 substrates of this enzyme are L-alanine, water, and nicotinamide adenine dinucleotide+, whereas its 4 products are pyruvate, ammonia, NADH, and hydrogen ion. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-alanine:NAD+ oxidoreductase. Other names in common use include AlaDH, L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle.

— Freebase

Retinal dehydrogenase

Retinal dehydrogenase

In enzymology, a retinal dehydrogenase is an enzyme that catalyzes the chemical reaction++ The 3 substrates of this enzyme are retinal, NAD+, and H2O, whereas its 3 products are retinoic acid, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is retinal:NAD+ oxidoreductase. This enzyme is also called cytosolic retinal dehydrogenase. This enzyme participates in retinol metabolism. It has 2 cofactors: FAD, and Metal.

— Freebase

Glycolaldehyde dehydrogenase

Glycolaldehyde dehydrogenase

In enzymology, a glycolaldehyde dehydrogenase is an enzyme that catalyzes the chemical reaction++ The 3 substrates of this enzyme are glycolaldehyde, NAD+, and H2O, whereas its 3 products are glycolate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycolaldehyde:NAD+ oxidoreductase. This enzyme is also called glycol aldehyde dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

— Freebase

FMN reductase

FMN reductase

In enzymology, an FMN reductase is an enzyme that catalyzes the chemical reaction+ The 3 substrates of this enzyme are FMNH2, NAD+, and NADP+, whereas its 4 products are FMN, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is FMNH2:NAD+ oxidoreductase. Other names in common use include NADH-FMN reductase, NADH-dependent FMN reductase, NADH:FMN oxidoreductase, NADH:flavin oxidoreductase, NADH2 dehydrogenase, NADH2:FMN oxidoreductase, SsuE, riboflavin mononucleotide reductase, flavine mononucleotide reductase, riboflavin mononucleotide reductase, flavin mononucleotide reductase, and riboflavine mononucleotide reductase.

— Freebase

Prephenate dehydrogenase

Prephenate dehydrogenase

In enzymology, a prephenate dehydrogenase is an enzyme that catalyzes the chemical reaction+ Thus, the two substrates of this enzyme are prephenate and NAD+, whereas its 3 products are 4-hydroxyphenylpyruvate, CO2, and NADH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is prephenate:NAD+ oxidoreductase. Other names in common use include hydroxyphenylpyruvate synthase, and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.

— Freebase

nadp

nicotinamide adenine dinucleotide phosphate, NADP

a coenzyme similar to NAD and present in most living cells but serves as a reductant in different metabolic processes

— Princeton's WordNet

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