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The midpoint potential of the NAD + /NADH redox pair is −0.32 volts, which makes NADH a moderately strong reducing agent. [7] The reaction is easily reversible, when NADH reduces another molecule and is re-oxidized to NAD +. This means the coenzyme can continuously cycle between the NAD + and NADH forms without being consumed. [5]
NAD is commonly called by other names, including NAD+ or NADH. These are both forms of NAD — NAD+ is the positively charged form, which has lost an electron, and NADH is the neutral form which ...
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP [1] [2] or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP + is the ...
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.
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".