Nicotinamide adenine dinucleotide phosphate

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Nicotinamide adenine dinucleotide phosphate
NADP+ phys.svg
Identifiers
CAS number 53-59-8 YesY
PubChem 5885
ChemSpider 5674 YesY
MeSH NADP
ChEBI CHEBI:44409 YesY
ChEMBL CHEMBL213053 N
Jmol-3D images Image 1
Properties
Molecular formula C21H29N7O17P3
Molar mass 744.41 g mol−1
Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
 N (verify) (what is: YesY/N?)
Infobox references

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN (triphosphopyridine nucleotide), is a coenzyme used in anabolic reactions, such as lipid and nucleic acid synthesis, which require NADPH as a reducing agent.

NADPH is the reduced form of NADP+. NADP+ differs from NAD+ in the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine moiety.

In plants[edit]

In photosynthetic organisms, NADPH is produced by ferredoxin-NADP+ reductase in the last step of the electron chain of the light reactions of photosynthesis. It is used as reducing power for the biosynthetic reactions in the Calvin cycle to assimilate carbon dioxide. It is used to help the carbon dioxide turn into glucose.

In animals[edit]

Synthesis[edit]

The major source of NADPH in animals and other non-photosynthetic organisms is the pentose phosphate pathway.

However, there are several other lesser-known mechanisms of generating NADPH, all of which depend on the presence of mitochondria. The key enzymes in these processes are: NADP-linked malic enzyme, NADP-linked isocitrate dehydrogenase, and nicotinamide nucleotide transhydrogenase.[1] The isocitrate dehydrogenase mechanism appears to be the major source of NADPH in fat and possibly also liver cells.[2] Also, in mitochondria, NADH kinase produces NADPH and ADP, using NADH and ATP as substrate.

Biological functions[edit]

NADPH provides the reducing equivalents for biosynthetic reactions and the oxidation-reduction involved in protecting against the toxicity of ROS (reactive oxygen species), allowing the regeneration of GSH (reduced glutathione).[3] NADPH is also used for anabolic pathways, such as lipid synthesis, cholesterol synthesis, and fatty acid chain elongation.

The NADPH system is also responsible for generating free radicals in immune cells. These radicals are used to destroy pathogens in a process termed the respiratory burst.[4] It is the source of reducing equivalents for cytochrome P450 hydroxylation of aromatic compounds, steroids, alcohols, and drugs.

Ball-and-stick models of NADP+ and NADPH
NADP+
NADP+ 
NADPH
NADPH 

See also[edit]

References[edit]

  1. ^ Hanukoglu, I; Rapoport, R (1995 Feb–May). "Routes and regulation of NADPH production in steroidogenic mitochondria". Endocrine research 21 (1–2): 231–41. doi:10.3109/07435809509030439. PMID 7588385. Retrieved 6 April 2012. 
  2. ^ Palmer, Michael. "10.4.3 Supply of NADPH for fatty acid synthesis". Metabolism Course Notes. Retrieved 6 April 2012. 
  3. ^ Rush, Glenn F.; Gorski, Joel R.; Ripple, Mary G.; Sowinski, Janice; Bugelski, Peter; Hewitt, William R. "Organic hydroperoxide-induced lipid peroxidation and cell death in isolated hepatocytes". Toxicology and Applied Pharmacology 78 (3): 473–483. doi:10.1016/0041-008X(85)90255-8. 
  4. ^ Ogawa, K.; Suzuki, K.; Okutsu, M.; Yamazaki, K.; Shinkai, S. (2008). "The association of elevated reactive oxygen species levels from neutrophils with low-grade inflammation in the elderly". Immun Ageing 5: 13. doi:10.1186/1742-4933-5-13. PMC 2582223. PMID 18950479.