flavin adenine dinucleotide

フラビンアデニンジヌクレオチド FAD

WordNet

1. (biochemistry) purine base found in DNA and RNA; pairs with thymine in DNA and with uracil in RNA (同)A
2. a ketone that forms the nucleus of certain natural yellow pigments like riboflavin

PrepTutorEJDIC

1. アデニン(肝臓・茶の葉から採れる塩基の一種)

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/05/20 13:23:20」(JST)

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[Wiki en表示]

"FAD" redirects here. For other uses, see FAD (disambiguation).

Flavin adenine dinucleotide
Identifiers
CAS number	146-14-5 Y
PubChem	643975
UNII	ZC44YTI8KK Y
EC number	205-663-1
DrugBank	DB03147
KEGG	D00005 N
MeSH	Flavin-Adenine+Dinucleotide
ChEBI	CHEBI:16238 Y
ChEMBL	CHEMBL1232663 N
Beilstein Reference	1208946
Gmelin Reference	108834
3DMet	B04619
Jmol-3D images	Image 1
SMILES CC1=CC2=C(C=C1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)OP(=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=NC6=C5N=CN=C6N)O)O)O)O)O
InChI InChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1 Y[PubChem] Key: VWWQXMAJTJZDQX-UYBVJOGSSA-N Y[PubChem]
Properties
Molecular formula	C27H33N9O15P2
Molar mass	785.55 g mol−1
Appearance	White, vitreous crystals
log P	-1.336
Acidity (pKa)	1.128
Basicity (pKb)	12.8689
N (verify) (what is: Y/N?) Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

In biochemistry, flavin adenine dinucleotide (FAD) is a redox cofactor involved in several important reactions in metabolism. FAD can exist in two different redox states, which it converts between by accepting or donating electrons. The molecule consists of a riboflavin moiety (vitamin B₂) bound to the phosphate group of an ADP molecule. The flavin group is bound to ribitol, a sugar alcohol, by a carbon-nitrogen bond, not a glycosidic bond. Thus, riboflavin is not technically a nucleotide; the name flavin adenine dinucleotide is a misnomer.

FAD can be reduced to FADH₂, whereby it accepts two hydrogen atoms (a net gain of two electrons):

FAD (fully oxidized form, or quinone form) accepts two electrons and two protons to become FADH₂ (hydroquinone form). FADH₂ can then be oxidized to the semireduced form (semiquinone) FADH by donating one electron and one proton. The semiquinone is then oxidized once more by losing an electron and a proton and is returned to the initial quinone form (FAD).

FAD is an aromatic ring system, whereas FADH₂ is not. This means that FADH₂ is significantly higher in energy, without the stabilization that aromatic structure provides. FADH₂ is an energy-carrying molecule, because, if it is oxidized, it will regain aromaticity and release all the energy represented by this stabilization.

The primary biochemical role of FADH₂ in eukaryotes is to carry high-energy electrons used for oxidative phosphorylation. Its hydrogens remain in the mitochondrial matrix, whilst FAD is tightly bound to a dehydrogenase enzyme i.e. the second protein complex in the oxidative phosphorylation chain. FAD is a prosthetic group in the enzyme complex succinate dehydrogenase (complex II) that oxidizes succinate to fumarate in the eighth step of the citric acid cycle. The high-energy electrons from this oxidation are stored momentarily by reducing FAD to FADH₂. FADH₂ then reverts to FAD, sending its two high-energy electrons through the electron transport chain; the energy in FADH₂ is enough to produce 1.5 equivalents of ATP by oxidative phosphorylation. Another metabolic source of FADH₂ is beta oxidation, where FAD serves as a coenzyme to acyl CoA dehydrogenase.

A flavoprotein is a protein that contains a flavin moiety, this may be in the form of FAD or FMN (Flavin mononucleotide) . There are many flavoproteins besides components of the succinate dehydrogenase complex, including α-ketoglutarate dehydrogenase and a component of the pyruvate dehydrogenase complex.

Additional images

• Riboflavin

• FADH2

• Adenine

See also

• Flavin mononucleotide
• NAD
• Thymidylate synthase (FAD), an enzyme that helps produce FAD

External links

• FAD bound to proteins in the PDB

References

UpToDate Contents

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• 1. 免疫不全症を引き起こすミエロペルオキシダーゼ欠損症および酵素白血球欠損症 myeloperoxidase deficiency and other enzymatic wbc defects causing immunodeficiency
• 2. ヘキソースリン酸側路およびグルタチオン代謝疾患（グルコース-6-リン酸脱水素酵素欠損症を除く） disorders of the hexose monophosphate shunt and glutathione metabolism other than glucose 6 phosphate dehydrogenase deficiency
• 3. 母体血中の無細胞核酸を使った非侵襲的出生前検査 noninvasive prenatal testing using cell free nucleic acids in maternal blood
• 4. 筋肉におけるエネルギー代謝 energy metabolism in muscle
• 5. 水溶性ビタミンの概要 overview of water soluble vitamins

English Journal

• Nitric oxide synthase inhibition and oxidative stress in cardiovascular diseases: Possible therapeutic targets?

• Rochette L, Lorin J, Zeller M, Guilland JC, Lorgis L, Cottin Y, Vergely C.SourceLaboratoire de Physiopathologie et Pharmacologies Cardio-Métaboliques (LPPCM), France. Electronic address: luc.rochette@u-bourgogne.fr.
• Pharmacology & therapeutics.Pharmacol Ther.2013 Dec;140(3):239-57. doi: 10.1016/j.pharmthera.2013.07.004. Epub 2013 Jul 13.
• Nitric oxide (NO) is synthetized enzymatically from l-arginine (l-Arg) by three NO synthase isoforms, iNOS, eNOS and nNOS. The synthesis of NO is selectively inhibited by guanidino-substituted analogs of l-Arg or methylarginines such as asymmetric dimethylarginine (ADMA), which results from protein
• PMID 23859953

• Characterizing the metabolic heterogeneity in human breast cancer xenografts by 3D high resolution fluorescence imaging.

• Xu HN, Zheng G, Tchou J, Nioka S, Li LZ.SourceMolecular Imaging Laboratory, Department of Radiology, Perelman School of Medicine, University of Pennsylvania, Pennsylvania, USA ; Britton Chance Laboratory of Redox Imaging, Johnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Pennsylvania, USA.
• SpringerPlus.Springerplus.2013 Dec;2(1):73. Epub 2013 Feb 28.
• We previously reported that tumor mitochondrial redox state and its heterogeneity distinguished between the aggressive and the indolent breast cancer xenografts, suggesting novel metabolic indices as biomarkers for predicting tumor metastatic potential. Additionally, we reported that the identified
• PMID 23543813

• The role of cyclophilin D in interspecies differences in susceptibility to hepatotoxic drug-induced mitochondrial injury.

• Sekine S, Kimura T, Motoyama M, Shitara Y, Wakazono H, Oida H, Horie T.SourceLaboratory of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8675, Japan.
• Biochemical pharmacology.Biochem Pharmacol.2013 Nov 15;86(10):1507-14. doi: 10.1016/j.bcp.2013.08.027. Epub 2013 Sep 3.
• Test compound A ((5Z)-6-[(2R,3S)-3-({[(4-Chloro-2-methylphenyl)sulfonyl]amino}methyl) bicyclo[2.2.2]oct-2-yl]hex-5-enoic acid) was withdrawn from premarketing clinical trials due to severe liver injury. Intracellular accumulation of lipids (steatosis) has been observed in human-derived cells and may
• PMID 24012842

Japanese Journal

• FTIR study of CPD photolyase with substrate in single strand DNA

• , , , , , ,
• BIOPHYSICS 11(0), 39-45, 2015
• … The cyclobutane pyrimidine dimer (CPD)-PHR binds flavin adenine dinucleotide (FAD) as a cofactor and repairs CPD lesions in double-stranded DNA. …
• NAID 130004940808

• Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH

• Seo Daisuke,Naito Hiroshi,Nishimura Erika,Sakurai Takeshi
• Photosynthesis Research xx(xx), xxxx-xxxx, 2015
• Ferredoxin-NAD(P)+ oxidoreductases ([EC 1.18.1.2], [EC 1.18.1.3], FNRs) from green sulfur bacteria, purple non-sulfur bacteria and most of Firmicutes, such as Bacillus subtilis (BsFNR) are homo-dimeri …
• NAID 120005602822

• Role of the C-terminal extension stacked on the re-face of the isoalloxazine ring moiety of the flavin adenine dinucleotide prosthetic group in ferredoxin-NADP+ oxidoreductase from Bacillus subtilis

• Seo Daisuke,Asano Tomoya,Komori Hirofumi,Sakurai Takeshi
• Plant Physiology and Biochemistry 81, 143-148, 2014-08
• … Ferredoxin-NADP+ oxidoreductase [EC 1.18.1.2] from Bacillus subtilis (BsFNR) is homologous to the bacterial NADPH-thioredoxin reductase, but possesses a unique C-terminal extension that covers the re-face of the isoalloxazine ring moiety of the flavin adenine dinucleotide (FAD) prosthetic group. …
• NAID 120005411656

Related Links

• Flavin adenine dinucleotide - DrugBank

Identification Name Flavin adenine dinucleotide Accession Number DB03147 (EXPT01391) Type Small Molecule Groups Approved Description A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various ...

• flavin adenine dinucleotide | C27H33N9O15P2 - PubChem

flavin adenine dinucleotide | C27H33N9O15P2 | CID 643975 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists NIH ...

Related Pictures

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★リンクテーブル★

リンク元	「フラビンアデニンジヌクレオチド」「FAD」「FMN」
拡張検索	「flavin-adenine dinucleotide sodium」「flavin-adenine dinucleotide」

「フラビンアデニンジヌクレオチド」

　　[★]

英

flavin adenine dinucleotide, FAD

化

フラビンアデニンジヌクレオチドナトリウム flavin-adenine dinucleotide sodium

商

FAD、アスルダム、アセラート、アデフラビン、アデラビン9号、エフエーミック、ヒシデニン、ビタスト、ファデミン、フラジレン、フラッド、フラビタン、ベマカスト、ムコティア、ムコファジン、ライボミンS、リバレス、レバサルト、ワカデニン

関

フラビン、リボフラビン = ビタミンB2。臓器製剤

• 酸化還元反応に関わる補酵素。
• 栄養ドリンクを飲んで尿が黄色に着色するのはフラビンのせい。
• H+をe-を受け取って還元力のキャリアーとなる。

「FAD」

　　[★] フラビンアデニンジヌクレオチド flavin adenine dinucleotide

「FMN」

　　[★] フラビンモノヌクレオチド flavin adenine dinucleotide

「flavin-adenine dinucleotide sodium」

　　[★]

フラビンアデニンジヌクレオチドナトリウム

関

FAD、flavin-adenine dinucleotide

「flavin-adenine dinucleotide」

　　[★]

フラビンアデニンジヌクレオチド

関

FAD、flavin-adenine dinucleotide sodium