You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Record Information
Version3.6
Creation Date2006-08-16 14:07:20 UTC
Update Date2013-05-29 19:31:21 UTC
HMDB IDHMDB01377
Secondary Accession NumbersNone
Metabolite Identification
Common NameOxygen
DescriptionOxygen is the third most abundant element in the universe after hydrogen and helium and the most abundant element by mass in the Earth's crust. Diatomic oxygen gas constitutes 20.9% of the volume of air. All major classes of structural molecules in living organisms, such as proteins, carbohydrates, and fats, contain oxygen, as do the major inorganic compounds that comprise animal shells, teeth, and bone. Oxygen in the form of O2 is produced from water by cyanobacteria, algae and plants during photosynthesis and is used in cellular respiration for all living organisms. Green algae and cyanobacteria in marine environments provide about 70% of the free oxygen produced on earth and the rest is produced by terrestrial plants. Oxygen is used in mitochondria to help generate adenosine triphosphate (ATP) during oxidative phosphorylation. For animals, a constant supply of oxygen is indispensable for cardiac viability and function. To meet this demand, an adult human, at rest, inhales 1.8 to 2.4 grams of oxygen per minute. This amounts to more than 6 billion tonnes of oxygen inhaled by humanity per year. At a resting pulse rate, the heart consumes approximately 8-15 ml O2/min/100 g tissue. This is significantly more than that consumed by the brain (approximately 3 ml O2/min/100 g tissue) and can increase to more than 70 ml O2/min/100 g myocardial tissue during vigorous exercise. As a general rule, mammalian heart muscle cannot produce enough energy under anaerobic conditions to maintain essential cellular processes; thus, a constant supply of oxygen is indispensable to sustain cardiac function and viability. However, the role of oxygen and oxygen-associated processes in living systems is complex, and they and can be either beneficial or contribute to cardiac dysfunction and death (through reactive oxygen species). Reactive oxygen species (ROS) are a family of oxygen-derived free radicals that are produced in mammalian cells under normal and pathologic conditions. Many ROS, such as the superoxide anion (O2-)and hydrogen peroxide (H2O2), act within blood vessels, altering mechanisms mediating mechanical signal transduction and autoregulation of cerebral blood flow. Reactive oxygen species are believed to be involved in cellular signaling in blood vessels in both normal and pathologic states. The major pathway for the production of ROS is by way of the one-electron reduction of molecular oxygen to form an oxygen radical, the superoxide anion (O2-). Within the vasculature there are several enzymatic sources of O2-, including xanthine oxidase, the mitochondrial electron transport chain, and nitric oxide (NO) synthases. Studies in recent years, however, suggest that the major contributor to O2- levels in vascular cells is the membrane-bound enzyme NADPH-oxidase. Produced O2- can react with other radicals, such as NO, or spontaneously dismutate to produce hydrogen peroxide (H2O2). In cells, the latter reaction is an important pathway for normal O2- breakdown and is usually catalyzed by the enzyme superoxide dismutase (SOD). Once formed, H2O2 can undergo various reactions, both enzymatic and nonenzymatic. The antioxidant enzymes catalase and glutathione peroxidase act to limit ROS accumulation within cells by breaking down H2O2 to H2O. Metabolism of H2O2 can also produce other, more damaging ROS. For example, the endogenous enzyme myeloperoxidase uses H2O2 as a substrate to form the highly reactive compound hypochlorous acid. Alternatively, H2O2 can undergo Fenton or Haber-Weiss chemistry, reacting with Fe2+/Fe3+ ions to form toxic hydroxyl radicals (-.OH). (PMID: 17027622 , 15765131 ).
Structure
Thumb
Synonyms
  1. Dioxygen
  2. Molecular oxygen
  3. O2
  4. Oxygen
  5. Oxygen molecule
Chemical FormulaO2
Average Molecular Weight31.9988
Monoisotopic Molecular Weight31.989829244
IUPAC Nameoxidanone
Traditional Nameoxygen
CAS Registry Number7782-44-7
SMILES
O=O
InChI Identifier
InChI=1S/O2/c1-2
InChI KeyMYMOFIZGZYHOMD-UHFFFAOYSA-N
Chemical Taxonomy
KingdomInorganic Compounds
Super ClassHomogeneous Non-metal Compounds
ClassOther Non-metal Organides
Sub ClassOther Non-metal Oxides
Other Descriptors
  • a non-metabolic compound(Cyc)
  • dioxygen(ChEBI)
Substituents
  • N/A
Direct ParentOther Non-metal Oxides
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Respiration, oxidation, signaling
ApplicationNot Available
Cellular locations
  • Extracellular
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Peroxisome
Physical Properties
StateLiquid
Experimental Properties
PropertyValueReference
Melting Point-218.4 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility37.5 mg/mL at 21 °CNot Available
LogP0.65HANSCH,C ET AL. (1995)
Predicted Properties
PropertyValueSource
logP-0.28ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area34.14ChemAxon
Rotatable Bond Count0ChemAxon
Refractivity2.89ChemAxon
Polarizability1.53ChemAxon
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Extracellular
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Peroxisome
Biofluid Locations
  • Blood
Tissue Location
  • All Tissues
Pathways
NameSMPDB LinkKEGG Link
Arachidonic Acid MetabolismSMP00075map00590
Carnitine SynthesisSMP00465Not Available
Catecholamine BiosynthesisSMP00012map00350
D-Arginine and D-Ornithine MetabolismSMP00036map00472
Degradation of SuperoxidesSMP00468Not Available
Ethanol DegradationSMP00449Not Available
Glycine and Serine MetabolismSMP00004map00260
Mitochondrial Electron Transport ChainSMP00355map00190
Phenylalanine and Tyrosine MetabolismSMP00008map00360
Plasmalogen SynthesisSMP00479Not Available
Riboflavin MetabolismSMP00070map00740
Vitamin K MetabolismSMP00464Not Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified6960.0 +/- 410.0 uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified5760.0 +/- 580.0 uMAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified5490.0 (2780.0-7410.0) uMNewborn (0-30 days old)BothNormal
    • Geigy Scientific ...
details
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 IDFDB022589
KNApSAcK IDNot Available
Chemspider ID952
KEGG Compound IDC00007
BioCyc IDCPD-6641
BiGG ID33493
Wikipedia LinkOxygen
NuGOwiki LinkHMDB01377
Metagene LinkHMDB01377
METLIN ID3195
PubChem Compound977
PDB IDOXY
ChEBI ID15379
References
Synthesis ReferenceWynn, Richard L. Production of hydrogen and oxygen by thermal disassociation of water. U.S. Pat. Appl. Publ. (2007), 26pp.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Carrier M, Denault A, Lavoie J, Perrault LP: Randomized controlled trial of pericardial blood processing with a cell-saving device on neurologic markers in elderly patients undergoing coronary artery bypass graft surgery. Ann Thorac Surg. 2006 Jul;82(1):51-5. Pubmed: 16798186
  2. Valadka AB, Furuya Y, Hlatky R, Robertson CS: Global and regional techniques for monitoring cerebral oxidative metabolism after severe traumatic brain injury. Neurosurg Focus. 2000 Nov 15;9(5):e3. Pubmed: 16821755
  3. Armonda RA, Vo AH, Bell R, Neal C, Campbell WW: Multimodal monitoring during emergency hemicraniectomy for vein of Labbe thrombosis. Neurocrit Care. 2006;4(3):241-4. Pubmed: 16757831
  4. Sassaroli A, deB Frederick B, Tong Y, Renshaw PF, Fantini S: Spatially weighted BOLD signal for comparison of functional magnetic resonance imaging and near-infrared imaging of the brain. Neuroimage. 2006 Nov 1;33(2):505-14. Epub 2006 Aug 30. Pubmed: 16945553
  5. Zhang YT, Geng ZJ, Zhang Q, Li W, Zhang J: Auditory cortical responses evoked by pure tones in healthy and sensorineural hearing loss subjects: functional MRI and magnetoencephalography. Chin Med J (Engl). 2006 Sep 20;119(18):1548-54. Pubmed: 16996009
  6. Ketcham EM, Cairns CB: Hemoglobin-based oxygen carriers: development and clinical potential. Ann Emerg Med. 1999 Mar;33(3):326-37. Pubmed: 10036348
  7. Capelli-Schellpfeffer M, Gerber GS: The use of hyperbaric oxygen in urology. J Urol. 1999 Sep;162(3 Pt 1):647-54. Pubmed: 10458334
  8. Weaver LK, Howe S, Hopkins R, Chan KJ: Carboxyhemoglobin half-life in carbon monoxide-poisoned patients treated with 100% oxygen at atmospheric pressure. Chest. 2000 Mar;117(3):801-8. Pubmed: 10713010
  9. Rooth G: Transcutaneous oxygen tension measurements in newborn infants. Pediatrics. 1975 Feb;55(2):232-5. Pubmed: 1090895
  10. Nath KA, Norby SM: Reactive oxygen species and acute renal failure. Am J Med. 2000 Dec 1;109(8):665-78. Pubmed: 11099687
  11. Kotecha S, Allen J: Oxygen therapy for infants with chronic lung disease. Arch Dis Child Fetal Neonatal Ed. 2002 Jul;87(1):F11-4. Pubmed: 12091281
  12. Van Heerebeek L, Meischl C, Stooker W, Meijer CJ, Niessen HW, Roos D: NADPH oxidase(s): new source(s) of reactive oxygen species in the vascular system? J Clin Pathol. 2002 Aug;55(8):561-8. Pubmed: 12147646
  13. Forman HJ, Torres M: Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am J Respir Crit Care Med. 2002 Dec 15;166(12 Pt 2):S4-8. Pubmed: 12471082
  14. Kemp PJ, Lewis A, Hartness ME, Searle GJ, Miller P, O'Kelly I, Peers C: Airway chemotransduction: from oxygen sensor to cellular effector. Am J Respir Crit Care Med. 2002 Dec 15;166(12 Pt 2):S17-24. Pubmed: 12471084
  15. Frey B, Shann F: Oxygen administration in infants. Arch Dis Child Fetal Neonatal Ed. 2003 Mar;88(2):F84-8. Pubmed: 12598492
  16. Wang C, Schwaitzberg S, Berliner E, Zarin DA, Lau J: Hyperbaric oxygen for treating wounds: a systematic review of the literature. Arch Surg. 2003 Mar;138(3):272-9; discussion 280. Pubmed: 12611573
  17. Ho AM, Lee A, Karmakar MK, Dion PW, Chung DC, Contardi LH: Heliox vs air-oxygen mixtures for the treatment of patients with acute asthma: a systematic overview. Chest. 2003 Mar;123(3):882-90. Pubmed: 12628892
  18. Rodrigo GJ, Rodrigo C, Pollack CV, Rowe B: Use of helium-oxygen mixtures in the treatment of acute asthma: a systematic review. Chest. 2003 Mar;123(3):891-6. Pubmed: 12628893
  19. Wangsa-Wirawan ND, Linsenmeier RA: Retinal oxygen: fundamental and clinical aspects. Arch Ophthalmol. 2003 Apr;121(4):547-57. Pubmed: 12695252
  20. Cohn SM: Oxygen therapeutics in trauma and surgery. J Trauma. 2003 May;54(5 Suppl):S193-8. Pubmed: 12768124
  21. Gordillo GM, Sen CK: Revisiting the essential role of oxygen in wound healing. Am J Surg. 2003 Sep;186(3):259-63. Pubmed: 12946829
  22. Deedwania PC, Carbajal EV: Role of myocardial oxygen demand in the pathogenesis of silent ischemia during daily life. Am J Cardiol. 1992 Nov 16;70(16):19F-24F. Pubmed: 1442597
  23. Listello D, Glauser F: COPD: primary care management with drug and oxygen therapies. Geriatrics. 1992 Dec;47(12):28-30, 35-8. Pubmed: 1446842
  24. McDonagh M, Helfand M, Carson S, Russman BS: Hyperbaric oxygen therapy for traumatic brain injury: a systematic review of the evidence. Arch Phys Med Rehabil. 2004 Jul;85(7):1198-204. Pubmed: 15241774
  25. Davis PG, Tan A, O'Donnell CP, Schulze A: Resuscitation of newborn infants with 100% oxygen or air: a systematic review and meta-analysis. Lancet. 2004 Oct 9-15;364(9442):1329-33. Pubmed: 15474135
  26. Roeckl-Wiedmann I, Bennett M, Kranke P: Systematic review of hyperbaric oxygen in the management of chronic wounds. Br J Surg. 2005 Jan;92(1):24-32. Pubmed: 15635604
  27. Goldstein BJ, Mahadev K, Wu X: Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets. Diabetes. 2005 Feb;54(2):311-21. Pubmed: 15677487
  28. Giordano FJ: Oxygen, oxidative stress, hypoxia, and heart failure. J Clin Invest. 2005 Mar;115(3):500-8. Pubmed: 15765131
  29. Jallali N, Withey S, Butler PE: Hyperbaric oxygen as adjuvant therapy in the management of necrotizing fasciitis. Am J Surg. 2005 Apr;189(4):462-6. Pubmed: 15820462
  30. Domachevsky L, Adir Y, Grupper M, Keynan Y, Bentur Y: Hyperbaric oxygen in the treatment of carbon monoxide poisoning. Clin Toxicol (Phila). 2005;43(3):181-8. Pubmed: 15902792
  31. Burkhoff D, Lefer DJ: Cardioprotection before revascularization in ischemic myocardial injury and the potential role of hemoglobin-based oxygen carriers. Am Heart J. 2005 Apr;149(4):573-9. Pubmed: 15990736
  32. Glazier JJ: Attenuation of reperfusion microvascular ischemia by aqueous oxygen: experimental and clinical observations. Am Heart J. 2005 Apr;149(4):580-4. Pubmed: 15990737
  33. Kevin LG, Novalija E, Stowe DF: Reactive oxygen species as mediators of cardiac injury and protection: the relevance to anesthesia practice. Anesth Analg. 2005 Nov;101(5):1275-87. Pubmed: 16243980
  34. Bennett M, Kertesz T, Yeung P: Hyperbaric oxygen therapy for idiopathic sudden sensorineural hearing loss and tinnitus: a systematic review of randomized controlled trials. J Laryngol Otol. 2005 Oct;119(10):791-8. Pubmed: 16259656
  35. Levy MM: Pathophysiology of oxygen delivery in respiratory failure. Chest. 2005 Nov;128(5 Suppl 2):547S-553S. Pubmed: 16306052
  36. Huang YC: Monitoring oxygen delivery in the critically ill. Chest. 2005 Nov;128(5 Suppl 2):554S-560S. Pubmed: 16306053
  37. Liu Z, Xiong T, Meads C: Clinical effectiveness of treatment with hyperbaric oxygen for neonatal hypoxic-ischaemic encephalopathy: systematic review of Chinese literature. BMJ. 2006 Aug 19;333(7564):374. Epub 2006 May 11. Pubmed: 16690641
  38. Friedman HI, Fitzmaurice M, Lefaivre JF, Vecchiolla T, Clarke D: An evidence-based appraisal of the use of hyperbaric oxygen on flaps and grafts. Plast Reconstr Surg. 2006 Jun;117(7 Suppl):175S-190S; discussion 191S-192S. Pubmed: 16799386
  39. Terashvili M, Pratt PF, Gebremedhin D, Narayanan J, Harder DR: Reactive oxygen species cerebral autoregulation in health and disease. Pediatr Clin North Am. 2006 Oct;53(5):1029-37, xi. Pubmed: 17027622
  40. Colebourn CL, Barber V, Young JD: Use of helium-oxygen mixture in adult patients presenting with exacerbations of asthma and chronic obstructive pulmonary disease: a systematic review. Anaesthesia. 2007 Jan;62(1):34-42. Pubmed: 17156225
  41. Bradley JM, Lasserson T, Elborn S, Macmahon J, O'neill B: A systematic review of randomized controlled trials examining the short-term benefit of ambulatory oxygen in COPD. Chest. 2007 Jan;131(1):278-85. Pubmed: 17218587
  42. Tin W, Gupta S: Optimum oxygen therapy in preterm babies. Arch Dis Child Fetal Neonatal Ed. 2007 Mar;92(2):F143-7. Pubmed: 17337663
  43. Higgins RD, Bancalari E, Willinger M, Raju TN: Executive summary of the workshop on oxygen in neonatal therapies: controversies and opportunities for research. Pediatrics. 2007 Apr;119(4):790-6. Pubmed: 17403851
  44. Ness PM, Cushing MM: Oxygen therapeutics: pursuit of an alternative to the donor red blood cell. Arch Pathol Lab Med. 2007 May;131(5):734-41. Pubmed: 17488158
  45. Shelley KH: Photoplethysmography: beyond the calculation of arterial oxygen saturation and heart rate. Anesth Analg. 2007 Dec;105(6 Suppl):S31-6, tables of contents. Pubmed: 18048895
  46. Claure N: Automated regulation of inspired oxygen in preterm infants: oxygenation stability and clinician workload. Anesth Analg. 2007 Dec;105(6 Suppl):S37-41. Pubmed: 18048896
  47. Toffaletti J, Zijlstra WG: Misconceptions in reporting oxygen saturation. Anesth Analg. 2007 Dec;105(6 Suppl):S5-9. Pubmed: 18048899
  48. Ferrari R, Ceconi C, Curello S, Cargnoni A, Pasini E, De Giuli F, Albertini A: Role of oxygen free radicals in ischemic and reperfused myocardium. Am J Clin Nutr. 1991 Jan;53(1 Suppl):215S-222S. Pubmed: 1845919
  49. Kindwall EP, Gottlieb LJ, Larson DL: Hyperbaric oxygen therapy in plastic surgery: a review article. Plast Reconstr Surg. 1991 Nov;88(5):898-908. Pubmed: 1924583
  50. Cain SM, Curtis SE: Experimental models of pathologic oxygen supply dependency. Crit Care Med. 1991 May;19(5):603-12. Pubmed: 2026022
  51. Weg JG: Oxygen transport in adult respiratory distress syndrome and other acute circulatory problems: relationship of oxygen delivery and oxygen consumption. Crit Care Med. 1991 May;19(5):650-7. Pubmed: 2026027
  52. Edwards JD: Oxygen transport in cardiogenic and septic shock. Crit Care Med. 1991 May;19(5):658-63. Pubmed: 2026028
  53. Tuchschmidt J, Oblitas D, Fried JC: Oxygen consumption in sepsis and septic shock. Crit Care Med. 1991 May;19(5):664-71. Pubmed: 2026029
  54. Reilly PM, Schiller HJ, Bulkley GB: Pharmacologic approach to tissue injury mediated by free radicals and other reactive oxygen metabolites. Am J Surg. 1991 Apr;161(4):488-503. Pubmed: 2035771
  55. Burton GG, Wagshul FA, Henderson D, Kime SW: Fatal airway obstruction caused by a mucous ball from a transtracheal oxygen catheter. Chest. 1991 Jun;99(6):1520-3. Pubmed: 2036843
  56. McCord JM, Fridovich I: The biology and pathology of oxygen radicals. Ann Intern Med. 1978 Jul;89(1):122-7. Pubmed: 208444
  57. Ardehali A, Ports TA: Myocardial oxygen supply and demand. Chest. 1990 Sep;98(3):699-705. Pubmed: 2203620
  58. Edwards JD: Practical application of oxygen transport principles. Crit Care Med. 1990 Jan;18(1 Pt 2):S45-8. Pubmed: 2403513
  59. Kloner RA, Przyklenk K, Whittaker P: Deleterious effects of oxygen radicals in ischemia/reperfusion. Resolved and unresolved issues. Circulation. 1989 Nov;80(5):1115-27. Pubmed: 2553296
  60. Dart RC, Sanders AB: Oxygen free radicals and myocardial reperfusion injury. Ann Emerg Med. 1988 Jan;17(1):53-8. Pubmed: 3276245
  61. Cross CE, Halliwell B, Borish ET, Pryor WA, Ames BN, Saul RL, McCord JM, Harman D: Oxygen radicals and human disease. Ann Intern Med. 1987 Oct;107(4):526-45. Pubmed: 3307585
  62. Gabb G, Robin ED: Hyperbaric oxygen. A therapy in search of diseases. Chest. 1987 Dec;92(6):1074-82. Pubmed: 3315479
  63. Jackson RM: Pulmonary oxygen toxicity. Chest. 1985 Dec;88(6):900-5. Pubmed: 3905287
  64. Vik-Mo H, Mjos OD: Influence of free fatty acids on myocardial oxygen consumption and ischemic injury. Am J Cardiol. 1981 Aug;48(2):361-5. Pubmed: 6115579
  65. Klebanoff SJ: Oxygen metabolism and the toxic properties of phagocytes. Ann Intern Med. 1980 Sep;93(3):480-9. Pubmed: 6254418
  66. Tinits P: Oxygen therapy and oxygen toxicity. Ann Emerg Med. 1983 May;12(5):321-8. Pubmed: 6414343
  67. Lucey JF, Dangman B: A reexamination of the role of oxygen in retrolental fibroplasia. Pediatrics. 1984 Jan;73(1):82-96. Pubmed: 6419199
  68. Riley DJ, Berg RA, Edelman NH, Prockop DJ: Prevention of collagen deposition following pulmonary oxygen toxicity in the rat by cis-4-hydroxy-L-proline. J Clin Invest. 1980 Mar;65(3):643-51. Pubmed: 6986411
  69. DeVenuto F: Hemoglobin solutions as oxygen-delivering resuscitation fluids. Crit Care Med. 1982 Apr;10(4):238-45. Pubmed: 7039970
  70. Vlessis AA, Goldman RK, Trunkey DD: New concepts in the pathophysiology of oxygen metabolism during sepsis. Br J Surg. 1995 Jul;82(7):870-6. Pubmed: 7648095
  71. Seger D, Welch L: Carbon monoxide controversies: neuropsychologic testing, mechanism of toxicity, and hyperbaric oxygen. Ann Emerg Med. 1994 Aug;24(2):242-8. Pubmed: 8037390
  72. Frei B: Reactive oxygen species and antioxidant vitamins: mechanisms of action. Am J Med. 1994 Sep 26;97(3A):5S-13S; discussion 22S-28S. Pubmed: 8085584
  73. Jeroudi MO, Hartley CJ, Bolli R: Myocardial reperfusion injury: role of oxygen radicals and potential therapy with antioxidants. Am J Cardiol. 1994 Mar 10;73(6):2B-7B. Pubmed: 8141076
  74. Spahn DR, Leone BJ, Reves JG, Pasch T: Cardiovascular and coronary physiology of acute isovolemic hemodilution: a review of nonoxygen-carrying and oxygen-carrying solutions. Anesth Analg. 1994 May;78(5):1000-21. Pubmed: 8160966
  75. Helfman T, Falanga V: Gene expression in low oxygen tension. Am J Med Sci. 1993 Jul;306(1):37-41. Pubmed: 8328508
  76. Rudge FW: Carbon monoxide poisoning in infants: treatment with hyperbaric oxygen. South Med J. 1993 Mar;86(3):334-7. Pubmed: 8451675
  77. Ackerman WE 3rd, Molnar JM, Juneja MM: Beneficial effect of epidural anesthesia on oxygen consumption in a parturient with adult respiratory distress syndrome. South Med J. 1993 Mar;86(3):361-4. Pubmed: 8451680
  78. Haapaniemi T, Nylander G, Sirsjo A, Larsson J: Hyperbaric oxygen reduces ischemia-induced skeletal muscle injury. Plast Reconstr Surg. 1996 Mar;97(3):602-7; discussion 608-9. Pubmed: 8596792
  79. Heyland DK, Cook DJ, King D, Kernerman P, Brun-Buisson C: Maximizing oxygen delivery in critically ill patients: a methodologic appraisal of the evidence. Crit Care Med. 1996 Mar;24(3):517-24. Pubmed: 8625644
  80. Kerr ME, Bender CM, Monti EJ: An introduction to oxygen free radicals. Heart Lung. 1996 May-Jun;25(3):200-9; quiz 210-1. Pubmed: 8635921
  81. O'Donohue WJ Jr: Home oxygen therapy. Med Clin North Am. 1996 May;80(3):611-22. Pubmed: 8637306
  82. Cornwell EE 3rd, Kennedy F, Rodriguez J: The critical care of the severely injured patient--I. Assessing and improving oxygen delivery. Surg Clin North Am. 1996 Aug;76(4):959-69. Pubmed: 8782482
  83. Powell JF, Menon DK, Jones JG: The effects of hypoxaemia and recommendations for postoperative oxygen therapy. Anaesthesia. 1996 Aug;51(8):769-72. Pubmed: 8795322
  84. Dean E: Oxygen transport deficits in systemic disease and implications for physical therapy. Phys Ther. 1997 Feb;77(2):187-202. Pubmed: 9037219
  85. Feuerstein G, Yue TL, Ma X, Ruffolo RR: Novel mechanisms in the treatment of heart failure: inhibition of oxygen radicals and apoptosis by carvedilol. Prog Cardiovasc Dis. 1998 Jul-Aug;41(1 Suppl 1):17-24. Pubmed: 9715819
  86. Naito Y, Yoshikawa T, Yoshida N, Kondo M: Role of oxygen radical and lipid peroxidation in indomethacin-induced gastric mucosal injury. Dig Dis Sci. 1998 Sep;43(9 Suppl):30S-34S. Pubmed: 9753223
  87. Goodnough LT, Scott MG, Monk TG: Oxygen carriers as blood substitutes. Past, present, and future. Clin Orthop Relat Res. 1998 Dec;(357):89-100. Pubmed: 9917705

Only showing the first 50 proteins. There are 203 proteins in total.

Enzymes

General function:
Involved in oxidoreductase activity
Specific function:
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.
Gene Name:
TYR
Uniprot ID:
P14679
Molecular weight:
60392.69
Reactions
L-Dopa + Oxygen → Dopaquinone + Waterdetails
L-Tyrosine + Oxygen → Dopaquinone + Waterdetails
L-Tyrosine + Oxygen → L-Dopa + Waterdetails
L-Dopa + L-Tyrosine + Oxygen → Dopaquinone + L-Dopa + Waterdetails
Hydroquinone + Oxygen → Quinone + Waterdetails
Tyramine + Oxygen + NADH + Hydrogen Ion → Dopamine + NAD + Waterdetails
(S)-N-Methylcoclaurine + Oxygen + Reduced acceptor → (S)-3-Hydroxy-N-methylcoclaurine + Water + Acceptordetails
5,6-Dihydroxyindole + Oxygen → Indole-5,6-quinone + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Metabolizes sarcosine, L-pipecolic acid and L-proline.
Gene Name:
PIPOX
Uniprot ID:
Q9P0Z9
Molecular weight:
44065.515
Reactions
Sarcosine + Water + Oxygen → Glycine + Formaldehyde + Hydrogen peroxidedetails
L-Pipecolic acid + Oxygen → (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + Hydrogen peroxidedetails
General function:
Amino acid transport and metabolism
Specific function:
Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs.
Gene Name:
PAOX
Uniprot ID:
Q6QHF9
Molecular weight:
55512.64
Reactions
N1-Acetylspermine + Oxygen + Water → Spermidine + Acetamidopropanal + Hydrogen peroxidedetails
N1-Acetylspermidine + Oxygen + Water → Putrescine + Acetamidopropanal + Hydrogen peroxidedetails
N1,N12-Diacetylspermine + Oxygen + Water → N1-Acetylspermidine + 3-Acetamidobutanal + Hydrogen peroxidedetails
General function:
Involved in oxidoreductase activity
Specific function:
Not Available
Gene Name:
AOX1
Uniprot ID:
Q06278
Molecular weight:
147916.735
Reactions
An aldehyde + Water + Oxygen → a carboxylate + Hydrogen peroxidedetails
Pyridoxal + Oxygen + Water → 4-Pyridoxic acid + Hydrogen peroxidedetails
Gentisic acid + Hydrogen peroxide → Gentisate aldehyde + Oxygen + Waterdetails
Methylmalonic acid + Hydrogen peroxide → (S)-Methylmalonic acid semialdehyde + Oxygen + Waterdetails
1-Methylnicotinamide + Oxygen + Water → N1-Methyl-4-pyridone-3-carboxamide + Hydrogen peroxide + Hydrogen Iondetails
5-Hydroxyindoleacetaldehyde + Oxygen + Water → 5-Hydroxyindoleacetic acid + Hydrogen peroxidedetails
Citalopram aldehyde + Water + Oxygen → Citalopram propionic acid + Hydrogen peroxidedetails
1-Methylnicotinamide + Oxygen + Water → N1-Methyl-2-pyridone-5-carboxamide + Hydrogen peroxide + Hydrogen Iondetails
General function:
Involved in iron ion binding
Specific function:
Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol.
Gene Name:
SC5DL
Uniprot ID:
O75845
Molecular weight:
35300.55
Reactions
Lathosterol + NAD(P)H + Oxygen → 7-Dehydrocholesterol + NAD(P)(+) + Waterdetails
Lathosterol + NADH + Hydrogen Ion + Oxygen → 7-Dehydrocholesterol + NAD + Waterdetails
Lathosterol + NADPH + Hydrogen Ion + Oxygen → 7-Dehydrocholesterol + NADP + Waterdetails
General function:
Involved in flavin-containing monooxygenase activity
Specific function:
In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.
Gene Name:
FMO5
Uniprot ID:
P49326
Molecular weight:
32480.04
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Waterdetails
Trimethylamine + NADPH + Hydrogen Ion + Oxygen → Trimethylamine N-oxide + NADP + Waterdetails
Tamoxifen + Oxygen + NADPH + Hydrogen Ion → Tamoxifen N-oxide + NADP + Waterdetails
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
Acyl-CoA + Oxygen → trans-2,3-dehydroacyl-CoA + Hydrogen peroxidedetails
General function:
Involved in D-amino-acid oxidase activity
Specific function:
Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.
Gene Name:
DDO
Uniprot ID:
Q99489
Molecular weight:
40992.53
Reactions
D-Aspartic acid + Water + Oxygen → Oxalacetic acid + Ammonia + Hydrogen peroxidedetails
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
Heme + AH(2) + Oxygen → Biliverdin + Fe2+ + CO + A + Waterdetails
Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Fe3+ + FAD + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway.
Gene Name:
SQLE
Uniprot ID:
Q14534
Molecular weight:
63922.505
Reactions
Squalene + NADPH + Oxygen → (3S)-2,3-epoxy-2,3-dihydrosqualene + NADP + Waterdetails
Squalene + Reduced acceptor + Oxygen → (3S)-2,3-epoxy-2,3-dihydrosqualene + Acceptor + Waterdetails
Squalene + Oxygen + NADPH + Hydrogen Ion → (3S)-2,3-epoxy-2,3-dihydrosqualene + NADP + Waterdetails
General function:
Involved in flavin-containing monooxygenase activity
Specific function:
Catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. Inactive toward certain tertiary amines, such as imipramine or chloropromazine. Can catalyze the S-oxidation of methimazole. The truncated form is catalytically inactive.
Gene Name:
FMO2
Uniprot ID:
Q99518
Molecular weight:
53643.29
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Waterdetails
Trimethylamine + NADPH + Hydrogen Ion + Oxygen → Trimethylamine N-oxide + NADP + Waterdetails
Tamoxifen + Oxygen + NADPH + Hydrogen Ion → Tamoxifen N-oxide + NADP + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.
Gene Name:
MAOB
Uniprot ID:
P27338
Molecular weight:
58762.475
Reactions
RCH(2)NHR' + Water + Oxygen → RCHO + R'NH(2) + Hydrogen peroxidedetails
Tryptamine + Water + Oxygen → Indoleacetaldehyde + Ammonia + Hydrogen peroxidedetails
Tyramine + Water + Oxygen → 4-Hydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Aminoacetone + Water + Oxygen → Pyruvaldehyde + Ammonia + Hydrogen peroxidedetails
Norepinephrine + Water + Oxygen → 3,4-Dihydroxymandelaldehyde + Ammonia + Hydrogen peroxidedetails
Phenylethylamine + Oxygen + Water → Phenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Serotonin + Water + Oxygen → 5-Hydroxyindoleacetaldehyde + Ammonia + Hydrogen peroxidedetails
Epinephrine + Water + Oxygen → 3,4-Dihydroxymandelaldehyde + Methylamine + Hydrogen peroxidedetails
N-Acetylputrescine + Water + Oxygen → N4-Acetylaminobutanal + Ammonia + Hydrogen peroxidedetails
Dopamine + Water + Oxygen → 3,4-Dihydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
1-Methylhistamine + Water + Oxygen → Methylimidazole acetaldehyde + Ammonia + Hydrogen peroxidedetails
3-Methoxytyramine + Water + Oxygen → Homovanillin + Hydrogen peroxide + Ammoniadetails
Normetanephrine + Water + Oxygen → 3-Methoxy-4-hydroxyphenylglycolaldehyde + Ammonia + Hydrogen peroxidedetails
Metanephrine + Water + Oxygen → 3-Methoxy-4-hydroxyphenylglycolaldehyde + Hydrogen peroxide + Methylaminedetails
3-Hydroxykynurenamine + Oxygen → Quinoline-4,8-diol + Ammonia + Hydrogen peroxidedetails
5-Hydroxykynurenamine + Water + Oxygen → 4,6-Dihydroxyquinoline + Ammonia + Hydrogen peroxide + Waterdetails
Citalopram + Oxygen + Water → Citalopram aldehyde + Dimethylamine + Hydrogen peroxidedetails
N-Desmethylcitalopram + Oxygen + Water → Citalopram aldehyde + Methylamine + Hydrogen peroxidedetails
Didemethylcitalopram + Water + Oxygen → Citalopram aldehyde + Ammonia + Hydrogen peroxidedetails
General function:
Involved in flavin-containing monooxygenase activity
Specific function:
This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.
Gene Name:
FMO4
Uniprot ID:
P31512
Molecular weight:
63342.055
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Waterdetails
Trimethylamine + NADPH + Hydrogen Ion + Oxygen → Trimethylamine N-oxide + NADP + Waterdetails
Tamoxifen + Oxygen + NADPH + Hydrogen Ion → Tamoxifen N-oxide + NADP + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.
Gene Name:
MAOA
Uniprot ID:
P21397
Molecular weight:
59681.27
Reactions
RCH(2)NHR' + Water + Oxygen → RCHO + R'NH(2) + Hydrogen peroxidedetails
Tryptamine + Water + Oxygen → Indoleacetaldehyde + Ammonia + Hydrogen peroxidedetails
Tyramine + Water + Oxygen → 4-Hydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Aminoacetone + Water + Oxygen → Pyruvaldehyde + Ammonia + Hydrogen peroxidedetails
Norepinephrine + Water + Oxygen → 3,4-Dihydroxymandelaldehyde + Ammonia + Hydrogen peroxidedetails
Phenylethylamine + Oxygen + Water → Phenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Serotonin + Water + Oxygen → 5-Hydroxyindoleacetaldehyde + Ammonia + Hydrogen peroxidedetails
Epinephrine + Water + Oxygen → 3,4-Dihydroxymandelaldehyde + Methylamine + Hydrogen peroxidedetails
N-Acetylputrescine + Water + Oxygen → N4-Acetylaminobutanal + Ammonia + Hydrogen peroxidedetails
Dopamine + Water + Oxygen → 3,4-Dihydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
1-Methylhistamine + Water + Oxygen → Methylimidazole acetaldehyde + Ammonia + Hydrogen peroxidedetails
3-Methoxytyramine + Water + Oxygen → Homovanillin + Hydrogen peroxide + Ammoniadetails
Normetanephrine + Water + Oxygen → 3-Methoxy-4-hydroxyphenylglycolaldehyde + Ammonia + Hydrogen peroxidedetails
Metanephrine + Water + Oxygen → 3-Methoxy-4-hydroxyphenylglycolaldehyde + Hydrogen peroxide + Methylaminedetails
3-Hydroxykynurenamine + Oxygen → Quinoline-4,8-diol + Ammonia + Hydrogen peroxidedetails
5-Hydroxykynurenamine + Water + Oxygen → 4,6-Dihydroxyquinoline + Ammonia + Hydrogen peroxide + Waterdetails
Citalopram + Oxygen + Water → Citalopram aldehyde + Dimethylamine + Hydrogen peroxidedetails
N-Desmethylcitalopram + Oxygen + Water → Citalopram aldehyde + Methylamine + Hydrogen peroxidedetails
Didemethylcitalopram + Water + Oxygen → Citalopram aldehyde + Ammonia + Hydrogen peroxidedetails
General function:
Involved in flavin-containing monooxygenase activity
Specific function:
Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Plays an important role in the metabolism of trimethylamine (TMA), via the production of TMA N-oxide (TMAO). Is also able to perform S-oxidation when acting on sulfide compounds.
Gene Name:
FMO3
Uniprot ID:
P31513
Molecular weight:
60032.975
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Waterdetails
Trimethylamine + NADPH + Oxygen → Trimethylamine N-oxide + NADP + Waterdetails
Trimethylamine + NADPH + Hydrogen Ion + Oxygen → Trimethylamine N-oxide + NADP + Waterdetails
Tamoxifen + Oxygen + NADPH + Hydrogen Ion → Tamoxifen N-oxide + NADP + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).
Gene Name:
XDH
Uniprot ID:
P47989
Molecular weight:
146422.99
Reactions
Xanthine + Water + Oxygen → Uric acid + Hydrogen peroxidedetails
Hypoxanthine + Oxygen + Water → Xanthine + Hydrogen peroxidedetails
1-Methylxanthine + Water + Oxygen → 1-Methyluric acid + Hydrogen peroxidedetails
Paraxanthine + Oxygen + Water → 1,7-Dimethyluric acid + Hydrogen peroxidedetails
Theobromine + Water + Oxygen → 3,7-Dimethyluric acid + Hydrogen peroxidedetails
7-Methylxanthine + Oxygen + Water → 7-Methyluric acid + Hydrogen peroxidedetails
Mercaptopurine + Water + Oxygen → 6-Thiourate + Hydrogen peroxidedetails
General function:
Involved in catalytic activity
Specific function:
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Gene Name:
DHODH
Uniprot ID:
Q02127
Molecular weight:
42866.93
General function:
Involved in flavin-containing monooxygenase activity
Specific function:
This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines.
Gene Name:
FMO1
Uniprot ID:
Q01740
Molecular weight:
60310.285
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Waterdetails
Trimethylamine + NADPH + Hydrogen Ion + Oxygen → Trimethylamine N-oxide + NADP + Waterdetails
Tamoxifen + Oxygen + NADPH + Hydrogen Ion → Tamoxifen N-oxide + NADP + Waterdetails
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
Acyl-CoA + Oxygen → trans-2,3-dehydroacyl-CoA + Hydrogen peroxidedetails
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
Heme + AH(2) + Oxygen → Biliverdin + Fe2+ + CO + A + Waterdetails
Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Fe3+ + FAD + Waterdetails
General function:
Involved in D-amino-acid oxidase activity
Specific function:
Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
Gene Name:
DAO
Uniprot ID:
P14920
Molecular weight:
39473.75
Reactions
A D-amino acid + Water + Oxygen → a 2-oxo acid + Ammonia + Hydrogen peroxidedetails
Glycine + Water + Oxygen → Glyoxylic acid + Ammonia + Hydrogen peroxidedetails
D-Ornithine + Water + Oxygen → 5-Amino-2-oxopentanoic acid + Ammonia + Hydrogen peroxidedetails
D-Proline + Oxygen → 1-Pyrroline-2-carboxylic acid + Hydrogen peroxidedetails
cis-4-Hydroxy-D-proline + Oxygen → 1-Pyrroline-4-hydroxy-2-carboxylate + Hydrogen peroxidedetails
Cephalosporin C + Water + Oxygen → (7R)-7-(5-Carboxy-5-oxopentanoyl)aminocephalosporinate + Ammonia + Hydrogen peroxidedetails
General function:
Involved in coproporphyrinogen oxidase activity
Specific function:
Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III.
Gene Name:
CPOX
Uniprot ID:
P36551
Molecular weight:
50151.605
Reactions
Coproporphyrinogen III + Oxygen + Hydrogen Ion → Protoporphyrinogen IX + CO(2) + Waterdetails
Coproporphyrinogen III + Oxygen → Protoporphyrinogen IX + Carbon dioxide + Waterdetails
General function:
Involved in monooxygenase activity
Specific function:
Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Gene Name:
PAM
Uniprot ID:
P19021
Molecular weight:
108402.425
Reactions
Peptidylglycine + Ascorbic acid + Oxygen → peptidyl(2-hydroxyglycine) + Dehydroascorbic acid + Waterdetails
General function:
Involved in monooxygenase activity
Specific function:
Conversion of dopamine to noradrenaline.
Gene Name:
DBH
Uniprot ID:
P09172
Molecular weight:
69064.45
Reactions
Dopamine + Ascorbic acid + Oxygen → xi-Norepinephrine + Dehydroascorbic acid + Waterdetails
Dopamine + Ascorbic acid + Oxygen → Norepinephrine + Dehydroascorbic acid + Waterdetails
General function:
Involved in iron ion binding
Specific function:
Not Available
Gene Name:
MSMO1
Uniprot ID:
Q15800
Molecular weight:
19470.325
Reactions
4,4-Dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + Oxygen → 4-beta-Hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)(+) + Waterdetails
4-beta-Hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + Oxygen → 3-beta-Hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)(+) + Waterdetails
3-beta-Hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + Oxygen → 3-beta-Hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) + Waterdetails
4,4-Dimethyl-5a-cholesta-8,24-dien-3-b-ol + NADPH + Hydrogen Ion + Oxygen → 4a-Carboxy-4b-methyl-5a-cholesta-8,24-dien-3b-ol + NADP + Waterdetails
4,4-Dimethyl-5a-cholesta-8,24-dien-3-b-ol + NADH + Hydrogen Ion + Oxygen → 3-beta-Hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD + Waterdetails
4,4-Dimethyl-5a-cholesta-8,24-dien-3-b-ol + NADPH + Hydrogen Ion + Oxygen → 3-beta-Hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NADP + Waterdetails
General function:
Involved in 3-beta-hydroxy-delta5-steroid dehydrogenase activity
Specific function:
Not Available
Gene Name:
NSDHL
Uniprot ID:
Q15738
Molecular weight:
41899.99
General function:
Involved in monooxygenase activity
Specific function:
Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
Gene Name:
CYP51A1
Uniprot ID:
Q16850
Molecular weight:
57277.81
Reactions
Obtusifoliol + Oxygen + NADPH → Delta 8,14 -Sterol + Formic acid + NADP + Waterdetails
Lanosterin + Oxygen + NADPH + Hydrogen Ion → 4,4-Dimethylcholesta-8,14,24-trienol + Formic acid + NADP + Waterdetails
Obtusifoliol + Oxygen + NADPH + Hydrogen Ion → Delta 8,14 -Sterol + Formic acid + NADP + Waterdetails
General function:
Involved in electron carrier activity
Specific function:
Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Gene Name:
PHYH
Uniprot ID:
O14832
Molecular weight:
38538.065
Reactions
Phytanoyl-CoA + Oxoglutaric acid + Oxygen → 2-Hydroxyphytanoyl-CoA + Succinic acid + CO(2)details
General function:
Involved in monooxygenase activity
Specific function:
Plays an important role in the physiology of adrenergic neurons.
Gene Name:
TH
Uniprot ID:
P07101
Molecular weight:
55611.26
Reactions
L-Tyrosine + L-erythro-tetrahydrobiopterin + Oxygen → L-Dopa + 4a-Hydroxytetrahydrobiopterindetails
L-erythro-tetrahydrobiopterin + L-Tyrosine + Oxygen → L-Dopa + 4a-Carbinolamine tetrahydrobiopterin + Waterdetails
General function:
Involved in amino acid binding
Specific function:
Not Available
Gene Name:
PAH
Uniprot ID:
P00439
Molecular weight:
51861.565
Reactions
L-Phenylalanine + L-erythro-tetrahydrobiopterin + Oxygen → L-Tyrosine + 4a-Hydroxytetrahydrobiopterindetails
L-erythro-tetrahydrobiopterin + L-Phenylalanine + Oxygen → 4a-Carbinolamine tetrahydrobiopterin + L-Tyrosine + Waterdetails
General function:
Involved in antioxidant activity
Specific function:
Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
Gene Name:
PRDX6
Uniprot ID:
P30041
Molecular weight:
25034.715
Reactions
L-Phenylalanine + Oxygen → 2-Phenylacetamide + Carbon dioxidedetails
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Gene Name:
P4HA2
Uniprot ID:
O15460
Molecular weight:
60632.19
Reactions
L-proline-[procollagen] + Oxoglutaric acid + Oxygen → trans-4-hydroxy-L-proline-[procollagen] + Succinic acid + CO(2)details
L-Proline + Oxoglutaric acid + Oxygen → 4-Hydroxyproline + Succinic acid + Carbon dioxidedetails
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Gene Name:
P4HA1
Uniprot ID:
P13674
Molecular weight:
60966.645
Reactions
L-proline-[procollagen] + Oxoglutaric acid + Oxygen → trans-4-hydroxy-L-proline-[procollagen] + Succinic acid + CO(2)details
L-Proline + Oxoglutaric acid + Oxygen → 4-Hydroxyproline + Succinic acid + Carbon dioxidedetails
General function:
Involved in oxidoreductase activity
Specific function:
Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O(2) and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA.
Gene Name:
SCD
Uniprot ID:
O00767
Molecular weight:
41522.28
Reactions
Stearoyl-CoA + ferrocytochrome b5 + Oxygen + Hydrogen Ion → Oleoyl-CoA + ferricytochrome b5 + Waterdetails
General function:
Involved in iron ion binding
Specific function:
Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Gene Name:
BBOX1
Uniprot ID:
O75936
Molecular weight:
44714.6
Reactions
4-Trimethylammoniobutanoic acid + Oxoglutaric acid + Oxygen → L-Carnitine + Succinic acid + CO(2)details
4-Trimethylammoniobutanoic acid + Oxoglutaric acid + Oxygen → L-Carnitine + Succinic acid + Carbon dioxidedetails
General function:
Involved in copper ion binding
Specific function:
Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.
Gene Name:
ABP1
Uniprot ID:
P19801
Molecular weight:
85377.1
Reactions
Histamine + Water + Oxygen → Imidazole-4-acetaldehyde + Ammonia + Hydrogen peroxidedetails
Putrescine + Oxygen + Water → 4-Aminobutyraldehyde + Ammonia + Hydrogen peroxidedetails
Tryptamine + Water + Oxygen → Indoleacetaldehyde + Ammonia + Hydrogen peroxidedetails
General function:
Involved in copper ion binding
Specific function:
Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis.
Gene Name:
AOC3
Uniprot ID:
Q16853
Molecular weight:
84621.27
Reactions
RCH(2)NH(2) + Water + Oxygen → RCHO + Ammonia + Hydrogen peroxidedetails
Tyramine + Water + Oxygen → 4-Hydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Aminoacetone + Water + Oxygen → Pyruvaldehyde + Ammonia + Hydrogen peroxidedetails
Phenylethylamine + Oxygen + Water → Phenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
1,3-Diaminopropane + Oxygen + Water → 3-Aminopropionaldehyde + Ammonia + Hydrogen peroxidedetails
N-Methylputrescine + Oxygen + Hydrogen Ion → 1-Methylpyrrolinium + Hydrogen peroxide + Ammoniadetails
Dopamine + Water + Oxygen → 3,4-Dihydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Methylamine + Oxygen + Water → Formaldehyde + Ammonia + Hydrogen peroxidedetails
Cadaverine + Water + Oxygen → 5-Aminopentanal + Ammonia + Hydrogen peroxidedetails
General function:
Involved in copper ion binding
Specific function:
Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina.
Gene Name:
AOC2
Uniprot ID:
O75106
Molecular weight:
80515.11
Reactions
RCH(2)NH(2) + Water + Oxygen → RCHO + Ammonia + Hydrogen peroxidedetails
Tyramine + Water + Oxygen → 4-Hydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Aminoacetone + Water + Oxygen → Pyruvaldehyde + Ammonia + Hydrogen peroxidedetails
Phenylethylamine + Oxygen + Water → Phenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
1,3-Diaminopropane + Oxygen + Water → 3-Aminopropionaldehyde + Ammonia + Hydrogen peroxidedetails
N-Methylputrescine + Oxygen + Hydrogen Ion → 1-Methylpyrrolinium + Hydrogen peroxide + Ammoniadetails
Dopamine + Water + Oxygen → 3,4-Dihydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxidedetails
Methylamine + Oxygen + Water → Formaldehyde + Ammonia + Hydrogen peroxidedetails
Cadaverine + Water + Oxygen → 5-Aminopentanal + Ammonia + Hydrogen peroxidedetails
General function:
Involved in monooxygenase activity
Specific function:
Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE).
Gene Name:
CYP4A11
Uniprot ID:
Q02928
Molecular weight:
59347.31
Reactions
Octane + reduced rubredoxin + Oxygen → Octanol + oxidized rubredoxin + Waterdetails
Fatty acid + Oxygen + Reduced flavoprotein → Glycolic acid + Oxidized flavoprotein + Waterdetails
Arachidonic acid + Oxygen + NADPH + Hydrogen Ion → 20-Hydroxyeicosatetraenoic acid + NADP + Waterdetails
Arachidonic acid + Oxygen + NADPH + Hydrogen Ion → 11,12-EpETrE + NADP + Waterdetails
All-trans-retinoic acid + NADPH + Hydrogen Ion + Oxygen → all-trans-18-Hydroxyretinoic acid + NADP + Waterdetails
General function:
Involved in heme binding
Specific function:
Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.
Gene Name:
IDO1
Uniprot ID:
P14902
Molecular weight:
45325.89
Reactions
D-Tryptophan + Oxygen → N'-Formylkynureninedetails
L-Tryptophan + Oxygen → L-Formylkynureninedetails
Oxitriptan + Oxygen → 5-Hydroxy-N-formylkynureninedetails
Serotonin + Oxygen → Formyl-5-hydroxykynurenaminedetails
Melatonin + Oxygen → Acetyl-N-formyl-5-methoxykynurenaminedetails
General function:
Involved in monooxygenase activity
Specific function:
Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB.
Gene Name:
CYP11B1
Uniprot ID:
P15538
Molecular weight:
57572.44
Reactions
A steroid + reduced adrenal ferredoxin + Oxygen → an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + Waterdetails
Progesterone + Reduced ferredoxin + Oxygen → 11b-Hydroxyprogesterone + Oxidized ferredoxin + Waterdetails
Reduced adrenal ferredoxin + Androstenedione + Oxygen → 11b-Hydroxyandrost-4-ene-3,17-dione + Oxidized adrenal ferredoxin + Waterdetails
Cortexolone + Reduced ferredoxin + Oxygen → Hydrocortisone + Oxidized ferredoxin + Waterdetails
17-Hydroxyprogesterone + Reduced ferredoxin + Oxygen → 21-Deoxycortisol + Oxidized ferredoxin + Waterdetails
Deoxycorticosterone + Reduced ferredoxin + Oxygen → Corticosterone + Oxidized ferredoxin + Waterdetails
17a,21-Dihydroxypreg-nenolone + Reduced ferredoxin + Oxygen → 11b,17a,21-Trihydroxypreg-nenolone + Oxidized ferredoxin + Waterdetails
Deoxycorticosterone + Reduced adrenal ferredoxin + Oxygen → Aldosterone + Oxidized adrenal ferredoxin + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Gene Name:
PLOD1
Uniprot ID:
Q02809
Molecular weight:
83549.55
Reactions
L-lysine-[procollagen] + Oxoglutaric acid + Oxygen → (2S,5R)-5-hydroxy-L-lysine-[procollagen] + Succinic acid + CO(2)details
Protein lysine + Oxoglutaric acid + Oxygen → Procollagen 5-hydroxy-L-lysine + Succinic acid + Carbon dioxide + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Gene Name:
PLOD2
Uniprot ID:
O00469
Molecular weight:
84685.07
Reactions
L-lysine-[procollagen] + Oxoglutaric acid + Oxygen → (2S,5R)-5-hydroxy-L-lysine-[procollagen] + Succinic acid + CO(2)details
Protein lysine + Oxoglutaric acid + Oxygen → Procollagen 5-hydroxy-L-lysine + Succinic acid + Carbon dioxide + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Gene Name:
PLOD3
Uniprot ID:
O60568
Molecular weight:
84784.505
Reactions
L-lysine-[procollagen] + Oxoglutaric acid + Oxygen → (2S,5R)-5-hydroxy-L-lysine-[procollagen] + Succinic acid + CO(2)details
Protein lysine + Oxoglutaric acid + Oxygen → Procollagen 5-hydroxy-L-lysine + Succinic acid + Carbon dioxide + Waterdetails
General function:
Involved in amino acid binding
Specific function:
Not Available
Gene Name:
TPH1
Uniprot ID:
P17752
Molecular weight:
50984.725
Reactions
L-Tryptophan + L-erythro-tetrahydrobiopterin + Oxygen → Oxitriptan + 4a-Hydroxytetrahydrobiopterindetails
L-erythro-tetrahydrobiopterin + L-Tryptophan + Oxygen → Oxitriptan + 4a-Carbinolamine tetrahydrobiopterin + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Gene Name:
FTMT
Uniprot ID:
Q8N4E7
Molecular weight:
27537.885
Reactions
Fe2+ + Hydrogen Ion + Oxygen → Fe3+ + Waterdetails
General function:
Involved in amino acid binding
Specific function:
Not Available
Gene Name:
TPH2
Uniprot ID:
Q8IWU9
Molecular weight:
56056.295
Reactions
L-Tryptophan + L-erythro-tetrahydrobiopterin + Oxygen → Oxitriptan + 4a-Hydroxytetrahydrobiopterindetails
L-erythro-tetrahydrobiopterin + L-Tryptophan + Oxygen → Oxitriptan + 4a-Carbinolamine tetrahydrobiopterin + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
Gene Name:
CP
Uniprot ID:
P00450
Molecular weight:
122204.45
Reactions
Fe2+ + Hydrogen Ion + Oxygen → Fe3+ + Waterdetails
General function:
Involved in monooxygenase activity
Specific function:
Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis.
Gene Name:
CYP7A1
Uniprot ID:
P22680
Molecular weight:
57660.155
Reactions
Cholesterol + NADPH + Oxygen → 7a-Hydroxycholesterol + NADP + Waterdetails
Cholesterol + Oxygen + NADPH + Hydrogen Ion → 7a-Hydroxycholesterol + NADP + Waterdetails
27-Hydroxycholesterol + NADPH + Hydrogen Ion + Oxygen → 7-a,27-Dihydroxycholesterol + NADP + Waterdetails
Dehydroepiandrosterone + Oxygen + NADPH + Hydrogen Ion → 7a-Hydroxydehydroepiandrosterone + NADP + Waterdetails
General function:
Involved in pyridoxamine-phosphate oxidase activity
Specific function:
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Gene Name:
PNPO
Uniprot ID:
Q9NVS9
Molecular weight:
29987.79
Reactions
Pyridoxamine 5'-phosphate + Water + Oxygen → Pyridoxal 5'-phosphate + Ammonia + Hydrogen peroxidedetails
Pyridoxine 5'-phosphate + Oxygen → Pyridoxal 5'-phosphate + Hydrogen peroxidedetails
Pyridoxamine + Water + Oxygen → Pyridoxal + Ammonia + Hydrogen peroxidedetails
Pyridoxine + Oxygen → Pyridoxal + Hydrogen peroxidedetails

Only showing the first 50 proteins. There are 203 proteins in total.