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Record Information
Version5.0
StatusExpected but not Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2021-09-14 14:58:04 UTC
HMDB IDHMDB0001197
Secondary Accession Numbers
Metabolite Identification
Common NameFADH
DescriptionFADH is the reduced form of flavin adenine dinucleotide (FAD). FAD is synthesized from riboflavin and two molecules of ATP. Riboflavin is phosphorylated by ATP to give riboflavin 5-phosphate (FMN). FAD is then formed from FMN by the transfer of an AMP moiety from a second molecule of ATP. FADH is generated in each round of fatty acid oxidation, and the fatty acyl chain is shortened by two carbon atoms as a result of these reactions; because oxidation is on the beta carbon, this series of reactions is called the beta-oxidation pathway. In the citric acid cycle, FADH is involved in the harvesting of high-energy electrons from carbon fuels; the citric acid cycle itself neither generates a large amount of ATP nor includes oxygen as a reactant. Instead, the citric acid cycle removes electrons from acetyl CoA and uses these electrons to form FADH.
Structure
Thumb
Synonyms
Chemical FormulaC27H35N9O15P2
Average Molecular Weight787.5656
Monoisotopic Molecular Weight787.172784519
IUPAC Name{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}[({[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-1H,2H,3H,4H,5H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy}(hydroxy)phosphoryl)oxy]phosphinic acid
Traditional Namefadh(.)
CAS Registry Number1910-41-4
SMILES
CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC3=C1N=CN=C3N)C1=C(N2)C(=O)NC(=O)N1
InChI Identifier
InChI=1S/C27H35N9O15P2/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/h3-4,8-9,14-16,19-21,26,32,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H2,33,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
InChI KeyYPZRHBJKEMOYQH-UYBVJOGSSA-N
Chemical Taxonomy
Description Belongs to the class of organic compounds known as flavin nucleotides. These are nucleotides containing a flavin moiety. Flavin is a compound that contains the tricyclic isoalloxazine ring system, which bears 2 oxo groups at the 2- and 4-positions.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
ClassFlavin nucleotides
Sub ClassNot Available
Direct ParentFlavin nucleotides
Alternative Parents
Substituents
  • Flavin nucleotide
  • Purine ribonucleoside diphosphate
  • Purine ribonucleoside monophosphate
  • Flavin
  • Pentose phosphate
  • Pentose-5-phosphate
  • Alkyldiarylamine
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Organic pyrophosphate
  • Pentose monosaccharide
  • Pteridine
  • Monosaccharide phosphate
  • Imidazopyrimidine
  • Purine
  • Aminopyrimidine
  • Monoalkyl phosphate
  • Pyrimidone
  • Imidolactam
  • Benzenoid
  • Phosphoric acid ester
  • Organic phosphoric acid derivative
  • N-substituted imidazole
  • Monosaccharide
  • Pyrimidine
  • Alkyl phosphate
  • Azole
  • Heteroaromatic compound
  • Tetrahydrofuran
  • Imidazole
  • Vinylogous amide
  • Urea
  • Lactam
  • Secondary alcohol
  • Secondary amine
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Polyol
  • Primary amine
  • Amine
  • Alcohol
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Organic oxide
  • Organopnictogen compound
  • Organic oxygen compound
  • Organooxygen compound
  • Organonitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Ontology
Physiological effectNot Available
Disposition
Source
Process
RoleNot Available
Physical Properties
StateSolid
Experimental Molecular Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Experimental Chromatographic PropertiesNot Available
Predicted Molecular Properties
Predicted Chromatographic Properties
Spectra
Biological Properties
Cellular LocationsNot Available
Biospecimen LocationsNot Available
Tissue LocationsNot Available
Pathways
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB030853
KNApSAcK IDNot Available
Chemspider ID393487
KEGG Compound IDC01352
BioCyc IDFADH2
BiGG ID132077
Wikipedia LinkFlavin adenine dinucleotide
METLIN ID6073
PubChem Compound446013
PDB IDNot Available
ChEBI ID17877
Food Biomarker OntologyNot Available
VMH IDFADH2
MarkerDB IDNot Available
Good Scents IDNot Available
References
Synthesis ReferenceKavakli I Halil; Sancar Aziz Analysis of the role of intraprotein electron transfer in photoreactivation by DNA photolyase in vivo. Biochemistry (2004), 43(48), 15103-10.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Zeller HD, Hille R, Jorns MS: Bacterial sarcosine oxidase: identification of novel substrates and a biradical reaction intermediate. Biochemistry. 1989 Jun 13;28(12):5145-54. [PubMed:2475174 ]
  2. Ramsey AJ, Alderfer JL, Jorns MS: Energy transduction during catalysis by Escherichia coli DNA photolyase. Biochemistry. 1992 Aug 11;31(31):7134-42. [PubMed:1643047 ]
  3. Ramsey AJ, Jorns MS: Effect of 5-deazaflavin on energy transduction during catalysis by Escherichia coli DNA photolyase. Biochemistry. 1992 Sep 15;31(36):8437-41. [PubMed:1390627 ]
  4. Jorns MS: DNA photorepair: chromophore composition and function in two classes of DNA photolyases. Biofactors. 1990 Oct;2(4):207-11. [PubMed:2282137 ]

Only showing the first 10 proteins. There are 14 proteins in total.

Enzymes

General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
ACADL
Uniprot ID:
P28330
Molecular weight:
47655.275
Reactions
Palmityl-CoA + FAD → (2E)-Hexadecenoyl-CoA + FADHdetails
Octanoyl-CoA + FAD → (2E)-Octenoyl-CoA + FADHdetails
Lauroyl-CoA + FAD → (2E)-Dodecenoyl-CoA + FADHdetails
Tetradecanoyl-CoA + FAD → (2E)-Tetradecenoyl-CoA + FADHdetails
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADHdetails
Decanoyl-CoA (n-C10:0CoA) + FAD → (2E)-Decenoyl-CoA + FADHdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
ACADS
Uniprot ID:
P16219
Molecular weight:
44296.705
Reactions
Butyryl-CoA + FAD → FADH + Crotonoyl-CoAdetails
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADHdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
This enzyme is specific for acyl chain lengths of 4 to 16.
Gene Name:
ACADM
Uniprot ID:
P11310
Molecular weight:
46587.98
Reactions
Propionyl-CoA + FAD → FADH + Acrylyl-CoAdetails
Butyryl-CoA + FAD → FADH + Crotonoyl-CoAdetails
Palmityl-CoA + FAD → (2E)-Hexadecenoyl-CoA + FADHdetails
Octanoyl-CoA + FAD → (2E)-Octenoyl-CoA + FADHdetails
Lauroyl-CoA + FAD → (2E)-Dodecenoyl-CoA + FADHdetails
Tetradecanoyl-CoA + FAD → (2E)-Tetradecenoyl-CoA + FADHdetails
Isovaleryl-CoA + FAD → 3-Methylcrotonyl-CoA + FADHdetails
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADHdetails
Decanoyl-CoA (n-C10:0CoA) + FAD → (2E)-Decenoyl-CoA + FADHdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.
Gene Name:
ACOX1
Uniprot ID:
Q15067
Molecular weight:
70135.205
Reactions
Butyryl-CoA + FAD → FADH + Crotonoyl-CoAdetails
Palmityl-CoA + FAD → (2E)-Hexadecenoyl-CoA + FADHdetails
Octanoyl-CoA + FAD → (2E)-Octenoyl-CoA + FADHdetails
Lauroyl-CoA + FAD → (2E)-Dodecenoyl-CoA + FADHdetails
Tetradecanoyl-CoA + FAD → (2E)-Tetradecenoyl-CoA + FADHdetails
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADHdetails
Decanoyl-CoA (n-C10:0CoA) + FAD → (2E)-Decenoyl-CoA + FADHdetails
OPC8-CoA + FAD → trans-2-Enoyl-OPC8-CoA + FADHdetails
OPC6-CoA + FAD → trans-2-Enoyl-OPC6-CoA + FADHdetails
OPC4-CoA + FAD → trans-2-Enoyl-OPC4-CoA + FADHdetails
Tetracosahexaenoyl CoA + FAD → Trans-2-all-cis-6,9,12,15,18,21-tetracosaheptaenoyl-CoA + FADHdetails
Tetracosapentaenoyl coenzyme A, n-6 + FAD → (2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA + FADHdetails
General function:
Involved in heme oxygenase (decyclizing) activity
Specific function:
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
Gene Name:
HMOX2
Uniprot ID:
P30519
Molecular weight:
36032.615
Reactions
Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Iron + FAD + Waterdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
IVD
Uniprot ID:
P26440
Molecular weight:
43055.325
Reactions
Isovaleryl-CoA + FAD → 3-Methylcrotonyl-CoA + FADHdetails
General function:
Involved in oxidoreductase activity, acting on the CH-CH group of donors
Specific function:
Oxidizes the CoA-esters of 2-methyl-branched fatty acids (By similarity).
Gene Name:
ACOX3
Uniprot ID:
O15254
Molecular weight:
69574.075
Reactions
Butyryl-CoA + FAD → FADH + Crotonoyl-CoAdetails
Palmityl-CoA + FAD → (2E)-Hexadecenoyl-CoA + FADHdetails
Octanoyl-CoA + FAD → (2E)-Octenoyl-CoA + FADHdetails
Lauroyl-CoA + FAD → (2E)-Dodecenoyl-CoA + FADHdetails
Tetradecanoyl-CoA + FAD → (2E)-Tetradecenoyl-CoA + FADHdetails
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADHdetails
Decanoyl-CoA (n-C10:0CoA) + FAD → (2E)-Decenoyl-CoA + FADHdetails
OPC8-CoA + FAD → trans-2-Enoyl-OPC8-CoA + FADHdetails
OPC6-CoA + FAD → trans-2-Enoyl-OPC6-CoA + FADHdetails
OPC4-CoA + FAD → trans-2-Enoyl-OPC4-CoA + FADHdetails
Tetracosahexaenoyl CoA + FAD → Trans-2-all-cis-6,9,12,15,18,21-tetracosaheptaenoyl-CoA + FADHdetails
Tetracosapentaenoyl coenzyme A, n-6 + FAD → (2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA + FADHdetails
General function:
Involved in calcium ion binding
Specific function:
Not Available
Gene Name:
GPD2
Uniprot ID:
P43304
Molecular weight:
80851.99
Reactions
Glycerol 3-phosphate + FAD → Dihydroxyacetone phosphate + FADHdetails
General function:
Involved in heme oxygenase (decyclizing) activity
Specific function:
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
Gene Name:
HMOX1
Uniprot ID:
P09601
Molecular weight:
32818.345
Reactions
Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Iron + FAD + Waterdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive.
Gene Name:
GCDH
Uniprot ID:
Q92947
Molecular weight:
48126.715
Reactions
Glutaryl-CoA + FAD → FADH + Crotonoyl-CoA + Carbon dioxidedetails

Only showing the first 10 proteins. There are 14 proteins in total.