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| Name | Riboflavin Monophosphate | ||||||||||||||||||||||||||||||||||||||||||
| Accession Number | DB03247 (EXPT01458) | ||||||||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||||||||
| Groups | experimental | ||||||||||||||||||||||||||||||||||||||||||
| Description | A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues. [PubChem] |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Salts | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand mixtures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Categories |
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| CAS number | 146-17-8 | ||||||||||||||||||||||||||||||||||||||||||
| Weight |
Average: 456.3438 Monoisotopic: 456.104614802 |
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| Chemical Formula | C17H21N4O9P | ||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=FVTCRASFADXXNN-YRGRVCCFSA-N | ||||||||||||||||||||||||||||||||||||||||||
| InChI |
InChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12-,14-/m1/s1
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| IUPAC Name |
{[(2R,3R,4R)-5-{7,8-dimethyl-2,4-dioxo-2H,3H,4H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy}phosphonic acid
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| SMILES |
CC1=CC2=C(C=C1C)N(C[C@@H](O)[C@@H](O)[C@H](O)COP(O)(O)=O)C1=NC(=O)NC(=O)C1=N2
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| Mass Spec | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Classes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacology | |||||||||||||||||||||||||||||||||||||||||||
| Indication | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Absorption | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Metabolism | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Toxicity | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Affected organisms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||||||||
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| Manufacturers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Packagers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Dosage forms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Prices | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Patents | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Properties | |||||||||||||||||||||||||||||||||||||||||||
| State | solid | ||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Predicted Properties |
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| References | |||||||||||||||||||||||||||||||||||||||||||
| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| External Links |
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| ATC Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| AHFS Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| PDB Entries | |||||||||||||||||||||||||||||||||||||||||||
| FDA label | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| MSDS | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Interactions | |||||||||||||||||||||||||||||||||||||||||||
| Drug Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Targets |
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1. Trimethylamine dehydrogenase Pharmacological action: unknownTrimethylamine + H(2)O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron- transferring flavoprotein Organism class: bacterialUniProt ID: P16099 ![]() Gene: tmd Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 2. Rubredoxin-oxygen oxidoreductase Pharmacological action: unknownCatalyzes the four-electron reduction of one oxygen molecule to two water molecules Organism class: bacterialUniProt ID: Q9F0J6 ![]() Gene: roo Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 3. Riboflavin kinase/FMN adenylyltransferase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9WZW1 ![]() Gene: TM_0857 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q51990 ![]() Gene: morB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 5. NADPH-flavin oxidoreductase Pharmacological action: unknownInvolved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction Organism class: bacterialUniProt ID: Q56691 ![]() Gene: frp Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 6. Ribosomal protein S6 kinase alpha-4 Pharmacological action: unknownOrganism class: human UniProt ID: O75676 ![]() Gene: RPS6KA4 SNPs: SNPJam Report ![]() References:
7. Phenazine biosynthesis protein phzG Pharmacological action: unknownInvolved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. Probably catalyzes the final step in the conversion of trans-2,3- dihydro-3-hydroxyanthranilic acid (DHHA) to phenazine-1-carboxylic acid (PCA) Organism class: bacterialUniProt ID: Q51793 ![]() Gene: phzG Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9I4D4 ![]() Gene: PA1204 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: human UniProt ID: Q9NYQ3 ![]() Gene: HAO2 SNPs: SNPJam Report ![]() References:
10. Trp repressor binding protein WrbA, putative Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9RYU4 ![]() Gene: DR_A0214 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 11. Flavodoxin-1 Pharmacological action: unknownLow-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase Organism class: bacterialUniProt ID: P61949 ![]() Gene: fldA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 12. Isopentenyl-diphosphate delta-isomerase Pharmacological action: unknownCatalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity) Organism class: bacterialUniProt ID: P50740 ![]() Gene: fni Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Can oxidize either NADH or NADPH with a preference for NADH. Can catalyze electron transfer from NADH to various electron acceptors which include, in addition to molecular oxygen, cytochrome c, 2,6 dichlorphenolindophenol, methylene blue, ferricyanide or P-nitroblue tetrazolium Organism class: bacterialUniProt ID: Q60049 ![]() Gene: nox Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Functions as a redox protein with a potential of -325 mV Organism class: bacterialUniProt ID: Q46604 ![]() Gene: DvMF_2023 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 15. Nitroreductase family protein Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q81EW9 ![]() Gene: BC_1844 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 16. NADPH--cytochrome P450 reductase Pharmacological action: unknownThis enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5 Organism class: humanUniProt ID: P16435 ![]() Gene: POR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
17. Phosphopantothenoylcysteine decarboxylase Pharmacological action: unknownNecessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'- phosphopantotheine Organism class: humanUniProt ID: Q96CD2 ![]() Gene: PPCDC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
18. PhzG Pharmacological action: unknownOrganism class: bacterial UniProt ID: O69755 ![]() Gene: phzG Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 19. Ferredoxin-dependent glutamate synthase 2 Pharmacological action: unknown2 L-glutamate + 2 oxidized ferredoxin = L- glutamine + 2-oxoglutarate + 2 reduced ferredoxin Organism class: bacterialUniProt ID: P55038 ![]() Gene: gltS Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 20. Pyridoxamine 5'-phosphate oxidase Pharmacological action: unknownOxidizes PNP and PMP into pyridoxal 5'-phosphate (PLP) Organism class: bacterialUniProt ID: P0AFI7 ![]() Gene: pdxH Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 21. Flavodoxin Pharmacological action: unknownLow-potential electron donor to a number of redox enzymes Organism class: bacterialUniProt ID: P00322 ![]() Protein Sequence: FASTA References: 22. Oxygen-insensitive NAD(P)H nitroreductase Pharmacological action: unknownReduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5- (aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species Organism class: bacterialUniProt ID: P38489 ![]() Gene: nfnB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate Organism class: bacterialUniProt ID: P0A2Y7 ![]() Gene: aroC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 24. 2,4-dienoyl-CoA reductase [NADPH] Pharmacological action: unknownCatalyzes the NADP-dependent reduction of 2,4-dienoyl- CoA to yield trans-2- enoyl-CoA Organism class: bacterialUniProt ID: P42593 ![]() Gene: fadH Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 25. Dihydroorotate dehydrogenase A Pharmacological action: unknown(S)-dihydroorotate + O(2) = orotate + H(2)O(2) Organism class: bacterialUniProt ID: Q53ZE5 ![]() Gene: pyrDA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 26. Flavin reductase Pharmacological action: unknownCatalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. Possible role in protecting cells from oxidative damage or in regulating iron metabolism. In the liver, converts biliverdin to bilirubin Organism class: humanUniProt ID: P30043 ![]() Gene: BLVRB ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids Organism class: humanUniProt ID: Q9UJM8 ![]() Gene: HAO1 ![]() Protein Sequence: FASTA SNPs: SNPJam Report ![]() References:
28. Pyridoxine-5'-phosphate oxidase Pharmacological action: unknownOxidizes PNP and PMP into pyridoxal 5'-phosphate (PLP) Organism class: humanUniProt ID: Q9NVS9 ![]() Gene: PNPO ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
29. Major NAD(P)H-flavin oxidoreductase Pharmacological action: unknownInvolved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Major FMN reductase. It is capable of using both NADH and NADPH as electron donors. As electron acceptor, FMN is the most effective, FAD is considerably effective, and riboflavin is the least effective Organism class: bacterialUniProt ID: P46072 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References:
Pharmacological action: unknown
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN) Organism class: humanUniProt ID: Q969G6 ![]() Gene: RFK ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
31. Oxygen-insensitive NADPH nitroreductase Pharmacological action: unknownReduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major component of the oxygen- insensitive nitroreductase activity in E.coli Organism class: bacterialUniProt ID: P17117 ![]() Gene: nfsA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 32. Nitric-oxide synthase, brain Pharmacological action: unknownProduces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter Organism class: humanUniProt ID: P29475 ![]() Gene: NOS1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
33. Dihydroorotate dehydrogenase Pharmacological action: unknown(S)-dihydroorotate + O(2) = orotate + H(2)O(2) Organism class: bacterialUniProt ID: P0A7E1 ![]() Gene: pyrD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 34. Dihydropyrimidine dehydrogenase [NADP+] Pharmacological action: unknownInvolved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil Organism class: humanUniProt ID: Q12882 ![]() Gene: DPYD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
35. Dihydroorotate dehydrogenase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: Q02127 ![]() Gene: DHODH ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
36. Pentaerythritol tetranitrate reductase Pharmacological action: unknownOrganism class: bacterial UniProt ID: P71278 ![]() Gene: onr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 37. FMN-dependent NADH-azoreductase Pharmacological action: unknownCatalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity (By similarity) Organism class: bacterialUniProt ID: P63462 ![]() Gene: azoR Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Catalyzes the removal of two reducing equivalents (oxidative decarboxylation) from the cysteine residue of the C- terminal meso-lanthionine of epidermin to form a --C==C-- double bond Organism class: bacterialUniProt ID: P30197 ![]() Gene: epiD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 39. FMN-dependent NADH-azoreductase Pharmacological action: unknownCatalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes Organism class: bacterialUniProt ID: P41407 ![]() Gene: azoR Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate Organism class: bacterialUniProt ID: P56122 ![]() Gene: aroC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 41. Flavodoxin Pharmacological action: unknownLow-potential electron donor to a number of redox enzymes Organism class: bacterialUniProt ID: P0A3D9 ![]() Gene: isiB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 42. Flavodoxin Pharmacological action: unknownLow-potential electron donor to a number of redox enzymes Organism class: bacterialUniProt ID: P00323 ![]() Gene: DVU_2680 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 43. Flavodoxin Pharmacological action: unknownLow-potential electron donor to a number of redox enzymes Organism class: bacterialUniProt ID: P10340 ![]() Gene: isiB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 44. Hypothetical protein SMU.260 Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q8DW21 ![]() Gene: SMU_260 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 45. YtnJ Pharmacological action: unknownOrganism class: bacterial UniProt ID: O34974 ![]() Gene: moxC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9WXV1 ![]() Gene: TM_0096 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 47. Protein nrdI Pharmacological action: unknownNot known; probably involved in ribonucleotide reductase function Organism class: bacterialUniProt ID: P50618 ![]() Gene: nrdI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 48. Probable aromatic acid decarboxylase Pharmacological action: unknownOrganism class: bacterial UniProt ID: P69772 ![]() Gene: pad1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 49. L(+)-mandelate dehydrogenase Pharmacological action: unknownReduction of L(+)-mandelate to benzoylformate Organism class: bacterialUniProt ID: P20932 ![]() Gene: mdlB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: O07529 ![]() Gene: azr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 51. Flavodoxin Pharmacological action: unknownLow-potential electron donor to a number of redox enzymes (By similarity) Organism class: bacterialUniProt ID: Q9ZK53 ![]() Gene: fldA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 52. Serine/threonine-protein kinase Sgk1 Pharmacological action: unknownProtein kinase that plays an important role in cellular stress response. Activates certain potassium, sodium, and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, neuronal excitability and renal sodium excretion. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Mediates cell survival signals, phosphorylates and negatively regulates pro-apoptotic FOXO3A. Phosphorylates NEDD4L, which leads to its inactivation and to the subsequent activation of various channels and transporters such as ENaC, KCNA3/Kv1.3 or EAAT1. Isoform 2 exhibited a greater effect on cell plasma membrane expression of ENaC and Na(+) transport than isoform 1 Organism class: humanUniProt ID: O00141 ![]() Gene: SGK1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
53. Oxygen-insensitive NAD(P)H nitroreductase Pharmacological action: unknownReduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred Organism class: bacterialUniProt ID: Q01234 ![]() Gene: nfnB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Has nitric oxide reductase activity in combination with Hrb; probably involved in nitrosative stress protection Organism class: bacterialUniProt ID: Q9FDN7 ![]() Gene: fprA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 55. Isopentenyl-diphosphate delta-isomerase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q746I8 ![]() Gene: fni Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() |
| Enzymes |
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1. NADPH--cytochrome P450 reductase This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5 UniProt ID: P16435![]() Gene: POR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() |
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