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Other names in common use include NAD+ pyrophosphorylase, adenosine triphosphate-nicotinamide mononucleotide transadenylase, ATP:NMN adenylyltransferase, diphosphopyridine nucleotide pyrophosphorylase, nicotinamide adenine dinucleotide pyrophosphorylase, nicotinamide mononucleotide adenylyltransferase, and NMN adenylyltransferase.
The balance between the oxidized and reduced forms of nicotinamide adenine dinucleotide is called the NAD + /NADH ratio. This ratio is an important component of what is called the redox state of a cell, a measurement that reflects both the metabolic activities and the health of cells. [26]
Thus, the two substrates of this enzyme are ATP and NADH, whereas its two products are ADP and NADPH. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:NADH 2'-phosphotransferase.
This category groups enzymes that use nicotinamide adenine dinucleotide (NAD + and its reduced form, NADH) in redox reactions. See also Category:NADPH-dependent enzymes.. In general, the NAD is not stably associated with the enzyme, being a coenzyme; hence, we call such enzymes "NADH-dependent" enzymes, rather than simply "NADH enzymes".
NADH + H + + acceptor ⇌ NAD + + reduced acceptor. NADH dehydrogenase is a flavoprotein that contains iron-sulfur centers. NADH dehydrogenase is used in the electron transport chain for generation of ATP. The EC term NADH dehydrogenase (quinone) (EC 1.6.5.11) is defined for NADH dehydrogenases that use a quinone (excluding ubiquinone) as the ...
NMNH (Dihydronicotinamide mononucleotide), also known as reduced nicotinamide mononucleotide. [1] Both NMNH and NMN increase NAD+ levels in the body. [1] NAD+ is a universal coenzyme that plays vital roles in nearly all living organisms functioning in various biological processes such as metabolism, cell signaling, gene regulation, and DNA repair.
In enzymology, a glutamate synthase (NADH) (EC 1.4.1.14) is an enzyme that catalyzes the chemical reaction. 2 L-glutamate + NAD + L-glutamine + 2-oxoglutarate + NADH + H + Glutamate synthase facilitates the ammonium assimilation pathway, which follows the enzymes, nitrite reductase and glutamine synthase. [1]
The 3 substrates of this enzyme are sn-glycerol 3-phosphate, NAD +, and NADP +, whereas its 4 products are glycerone phosphate, NADH, NADPH, 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.