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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2016-02-11 01:03:59 UTC
HMDB IDHMDB01197
Secondary Accession Numbers
  • HMDB06252
  • HMDB06358
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 harvesting of high-energy electrons from carbon fuels; 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. (Biochemistry. Berg, Jeremy M. Tymoczko, John L. and Stryer, Lubert. New York: W. H. Freeman and Co. 2002.).
Structure
Thumb
Synonyms
ValueSource
1,5-dihydro-FADChEBI
DIHYDROFLAVINE-adenine dinucleotideChEBI
Flavin adenine dinucleotide (reduced)ChEBI
1,5-dihydro-P-5-Ester with adenosineHMDB
1,5-dihydro-Riboflavin 5'-(trihydrogen diphosphate) p'->5'-ester with adenosineHMDB
Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazineHMDB
Adenosine 5'-(trihydrogen pyrophosphate), 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazineHMDB
Adenosine 5'-{3-[D-ribo-5-(7,8-dimethyl-2,4-dioxo-1,2,3,4,5,10-tetrahydrobenzo[g]pteridin-10-yl)-2,3,4-trihydroxypentyl] dihydrogen diphosphate}HMDB
Adenosine 5-(trihydrogen pyrophosphate)HMDB
Adenosine pyrophosphate 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazineHMDB
Adenosine pyrophosphate, 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazineHMDB
Adenosine pyrophosphate, 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazineHMDB
benzo[GR]Pteridine riboflavin 5'-(trihydrogen diphosphate) derivHMDB
benzo[g]Pteridine riboflavin 5'-(trihydrogen diphosphate) derivHMDB
dihydro-FADHMDB
FADH2HMDB
FDAHMDB
Flavin adenine dinucleotide reducedHMDB
Reduced flavine adenine dinucleotideHMDB
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}(hydroxy)phosphoryl)oxy]({[(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})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 KeyInChIKey=YPZRHBJKEMOYQH-UYBVJOGSSA-N
Chemical Taxonomy
DescriptionThis compound 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
  • Flavin
  • Alkyldiarylamine
  • N-glycosyl compound
  • Glycosyl compound
  • Pteridine
  • Organic pyrophosphate
  • Monosaccharide phosphate
  • 6-aminopurine
  • Purine
  • Imidazopyrimidine
  • Monoalkyl phosphate
  • Pyrimidone
  • Aminopyrimidine
  • Imidolactam
  • Benzenoid
  • Alkyl phosphate
  • Pyrimidine
  • Primary aromatic amine
  • Phosphoric acid ester
  • Organic phosphoric acid derivative
  • Organic phosphate
  • N-substituted imidazole
  • Monosaccharide
  • Saccharide
  • Heteroaromatic compound
  • Vinylogous amide
  • Oxolane
  • Imidazole
  • Azole
  • Urea
  • Tertiary amine
  • Secondary alcohol
  • Polyol
  • Lactam
  • 1,2-diol
  • Oxacycle
  • Azacycle
  • Organoheterocyclic compound
  • Secondary amine
  • Hydrocarbon derivative
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Amine
  • Alcohol
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Ontology
StatusExpected but not Quantified
Origin
  • Endogenous
Biofunction
  • Enzyme cofactor
ApplicationNot Available
Cellular locationsNot Available
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility2.65 mg/mLALOGPS
logP-0.93ALOGPS
logP-5.4ChemAxon
logS-2.5ALOGPS
pKa (Strongest Acidic)1.86ChemAxon
pKa (Strongest Basic)5ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count18ChemAxon
Hydrogen Donor Count11ChemAxon
Polar Surface Area355.76 Å2ChemAxon
Rotatable Bond Count13ChemAxon
Refractivity188.8 m3·mol-1ChemAxon
Polarizability72.42 Å3ChemAxon
Number of Rings6ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-000i-0001200900-b0740b3d33d50996ccdeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-000m-0105900000-3abff26d5bb35f8527b8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-000i-0931700000-73f360589a13230eea7aView in MoNA
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,1H] 2D NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
Biological Properties
Cellular LocationsNot Available
Biofluid LocationsNot Available
Tissue LocationNot Available
Pathways
NameSMPDB LinkKEGG Link
2-ketoglutarate dehydrogenase complex deficiencySMP00549Not Available
Citric Acid CycleSMP00057map00020
Congenital lactic acidosisSMP00546Not Available
Fumarase deficiencySMP00547Not Available
Glutaminolysis and CancerSMP02298Not Available
Glycerol Phosphate ShuttleSMP00124Not Available
Mitochondrial complex II deficiencySMP00548Not Available
Phospholipid BiosynthesisSMP00025map00564
Pyruvate dehydrogenase deficiency (E2)SMP00551Not Available
Pyruvate dehydrogenase deficiency (E3)SMP00550Not Available
The oncogenic action of 2-hydroxyglutarateSMP02291Not Available
The oncogenic action of D-2-hydroxyglutarate in Hydroxygluaricaciduria SMP02359Not Available
The oncogenic action of FumarateSMP02295Not Available
The oncogenic action of L-2-hydroxyglutarate in HydroxygluaricaciduriaSMP02358Not Available
The oncogenic action of SuccinateSMP02292Not Available
Warburg EffectSMP00654Not Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB022483
KNApSAcK IDNot Available
Chemspider ID393487
KEGG Compound IDC01352
BioCyc IDFADH2
BiGG ID132077
Wikipedia LinkFADH
NuGOwiki LinkHMDB01197
Metagene LinkHMDB01197
METLIN ID6073
PubChem Compound446013
PDB IDFDA
ChEBI ID17877
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. [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. [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. [1390627 ]
  4. Jorns MS: DNA photorepair: chromophore composition and function in two classes of DNA photolyases. Biofactors. 1990 Oct;2(4):207-11. [2282137 ]

Enzymes

General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
ACADL
Uniprot ID:
P28330
Molecular weight:
47655.275
Reactions
hexadecanoyl-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 + (E)-but-2-enoyl-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 + (E)-but-2-enoyl-CoAdetails
hexadecanoyl-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 + (E)-but-2-enoyl-CoAdetails
hexadecanoyl-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 + Fe3+ + 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 + (E)-but-2-enoyl-CoAdetails
hexadecanoyl-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 + Fe3+ + 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 + (E)-but-2-enoyl-CoA + Carbon dioxidedetails
General function:
Involved in catalytic activity
Specific function:
Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.
Gene Name:
BLVRB
Uniprot ID:
P30043
Molecular weight:
22119.215
Reactions
FAD + NADPH + Hydrogen Ion → FADH + NADPdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent.
Gene Name:
ACADSB
Uniprot ID:
P45954
Molecular weight:
47485.035
Reactions
Butyryl-CoA + FAD → FADH + (E)-but-2-enoyl-CoAdetails
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADHdetails
General function:
Involved in 2-hydroxyglutarate dehydrogenase activity
Specific function:
Not Available
Gene Name:
L2HGDH
Uniprot ID:
Q9H9P8
Molecular weight:
50315.58
Reactions
2-Hydroxyglutarate + FAD → Oxoglutaric acid + FADHdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons.
Gene Name:
ACADVL
Uniprot ID:
P49748
Molecular weight:
70389.58
Reactions
hexadecanoyl-CoA + FAD → (2E)-Hexadecenoyl-CoA + FADHdetails