What is the full name of NADPH
Nicotinamide adenine dinucleotide
|Surname||Nicotinamide adenine dinucleotide|
|Molecular formula||C.21H27N7O14P.2 (reduced form, betaine)|
|Molar mass||663.425 g / mol (reduced form, betaine)|
|Melting point||140-142 ° C (decomposition)|
|As far as possible and customary, SI units are used. Unless otherwise noted, the data given apply to standard conditions.|
Nicotinamide adenine dinucleotide, actually Nicotinic acid amide adenine dinucleotide (abbreviated NAD) is a coenzyme that transfers hydride ions (two electrons / one protons) and is involved in numerous redox reactions in the cell's metabolism.
The abbreviations are used by IUPAC / IUBMB NAD+ for the oxidized form, NADH suggested for the reduced form and NAD in general. Sometimes, however, one still finds NAD instead of NAD+ and NADH2 instead of NADH.
The coenzyme was also known under the name in the older specialist literature up to the early 1960s Diphosphopyridine nucleotide, abbreviated DPN, or under the name Codehydrogenase I. or Coenzyme I. known. In contrast to nicotinamide adenine dinucleotide phosphate (NADP+), an otherwise almost identical coenzyme, lacks a phosphate residue on the adenosine - namely on the 2'C atom of the ribose - of the dinucleotide.
NAD+ can be reduced to NADH by taking up two electrons and one proton.
NAD+ mostly serves as an oxidizing agent for the organism. Hence the ratio is NADH / NAD+ small (
The energy-rich, reduced form of NADH is created in catabolism (glycolysis and citric acid cycle). In the oxidative metabolism it serves as an energy-supplying coenzyme of the respiratory chain, whereby ATP is generated. When it is oxidized, it gradually releases the electrons previously absorbed in the catabolic glucose and / or fat metabolism and transfers them to oxygen in the context of the intracellular oxyhydrogen reaction. This creates NAD+ and water.
NAD+ acts as a coenzyme of dehydrogenases, e.g. B. Alcohol dehydrogenase (ADH), for the oxidation of alcohol.
NADH shows in contrast to NAD+ an absorption maximum at a wavelength of 340 nm. This is used by means of photometry to follow enzymatic reactions (e.g. determination of the turnover number) and to make quantitative statements about the amount of converted substrate or manufactured product. In addition to one-step reactions, coupled enzyme reactions can also be used, as long as they are irreversible and directed towards the end product.
- ↑ Römpp Chemistry Lexicon. Georg Thieme Verlag, Stuttgart / New York, 1995
Categories: Lovely fabric | Phosphoric acid ester | Purine | Coenzyme / cofactor
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