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Showing metabocard for Oxygen (HMDB0001377)

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Record Information
Version5.0
StatusDetected and Quantified
Creation Date2006-08-16 14:07:20 UTC
Update Date2023-02-21 17:15:38 UTC
HMDB IDHMDB0001377
Secondary Accession Numbers
  • HMDB01377
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
Data?1676999738
MOL3D MOLSDF3D SDFPDB3D PDBSMILESInChI

MOL for HMDB0001377 (Oxygen)

977
  Mrv1652309042000222D          

  2  1  0  0  0  0            999 V2000
    1.6500    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
    2.4750    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  2  0  0  0  0
M  END
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3D MOL for HMDB0001377 (Oxygen)

HMDB0001377
     RDKit          3D
Oxygen
  2  1  0  0  0  0  0  0  0  0999 V2000
    0.5733    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
   -0.5733    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  2  0
M  END
Download

3D SDF for HMDB0001377 (Oxygen)

977
  Mrv1652309042000222D          

  2  1  0  0  0  0            999 V2000
    1.6500    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
    2.4750    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  2  0  0  0  0
M  END
> <DATABASE_ID>
HMDB0001377

> <DATABASE_NAME>
hmdb

> <SMILES>
O=O

> <INCHI_IDENTIFIER>
InChI=1S/O2/c1-2

> <INCHI_KEY>
MYMOFIZGZYHOMD-UHFFFAOYSA-N

> <FORMULA>
O2

> <MOLECULAR_WEIGHT>
31.9988

> <EXACT_MASS>
31.989829244

> <JCHEM_ACCEPTOR_COUNT>
2

> <JCHEM_ATOM_COUNT>
2

> <JCHEM_AVERAGE_POLARIZABILITY>
1.528255145499405

> <JCHEM_BIOAVAILABILITY>
1

> <JCHEM_DONOR_COUNT>
0

> <JCHEM_FORMAL_CHARGE>
0

> <JCHEM_GHOSE_FILTER>
0

> <JCHEM_IUPAC>
dioxygen

> <JCHEM_LOGP>
-0.27723172999999995

> <JCHEM_MDDR_LIKE_RULE>
0

> <JCHEM_NUMBER_OF_RINGS>
0

> <JCHEM_PHYSIOLOGICAL_CHARGE>
0

> <JCHEM_POLAR_SURFACE_AREA>
34.14

> <JCHEM_REFRACTIVITY>
2.8858

> <JCHEM_ROTATABLE_BOND_COUNT>
0

> <JCHEM_RULE_OF_FIVE>
1

> <JCHEM_TRADITIONAL_IUPAC>
singlet oxygen

> <JCHEM_VEBER_RULE>
1

$$$$
Download

3D-SDF for HMDB0001377 (Oxygen)

HMDB0001377
     RDKit          3D
Oxygen
  2  1  0  0  0  0  0  0  0  0999 V2000
    0.5733    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
   -0.5733    0.0000    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  2  0
M  END
Download

PDB for HMDB0001377 (Oxygen)

HEADER    PROTEIN                                 04-SEP-20   NONE
TITLE     NULL                                                        
COMPND    MOLECULE: 977                                               
SOURCE    NULL                                                        
KEYWDS    NULL                                                        
EXPDTA    NULL                                                        
AUTHOR    Marvin                                                      
REVDAT   1   04-SEP-20         0                                  
HETATM    1  O   UNK     0       3.080   0.000   0.000  0.00  0.00           O+0
HETATM    2  O   UNK     0       4.620   0.000   0.000  0.00  0.00           O+0
CONECT    1    2                                                            
CONECT    2    1                                                            
MASTER        0    0    0    0    0    0    0    0    2    0    2    0
END
Download

3D PDB for HMDB0001377 (Oxygen)

COMPND    HMDB0001377
HETATM    1  O1  UNL     1       0.573   0.000   0.000  1.00  0.00           O  
HETATM    2  O2  UNL     1      -0.573   0.000   0.000  1.00  0.00           O  
CONECT    1    2    2
END
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SMILES for HMDB0001377 (Oxygen)

O=O
Download

INCHI for HMDB0001377 (Oxygen)

InChI=1S/O2/c1-2
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View in JSmolView Stereo Labels
Synonyms
ValueSource
[OO]ChEBI
DioxygeneChEBI
DisauerstoffChEBI
e 948ChEBI
e-948ChEBI
e948ChEBI
Molecular oxygenChEBI
O2ChEBI
OXYGEN moleculeChEBI
DioxygenHMDB
Oxygen-16HMDB
Oxygen 16HMDB
Chemical FormulaO2
Average Molecular Weight31.9988
Monoisotopic Molecular Weight31.989829244
IUPAC Namedioxygen
Traditional Namesinglet oxygen
CAS Registry Number7782-44-7
SMILES
O=O
InChI Identifier
InChI=1S/O2/c1-2
InChI KeyMYMOFIZGZYHOMD-UHFFFAOYSA-N
Chemical Taxonomy
Description Belongs to the class of inorganic compounds known as other non-metal oxides. These are inorganic compounds containing an oxygen atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen belongs to the class of 'other non-metals'.
KingdomInorganic compounds
Super ClassHomogeneous non-metal compounds
ClassOther non-metal organides
Sub ClassOther non-metal oxides
Direct ParentOther non-metal oxides
Alternative Parents
Substituents
  • Other non-metal oxide
  • Inorganic oxide
Molecular FrameworkNot Available
External Descriptors
Ontology
Physiological effectNot Available
Disposition
Biological locationRoute of exposureSource
Process
Naturally occurring process
Role
Industrial application
Physical Properties
StateLiquid
Experimental Molecular 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)
Experimental Chromatographic PropertiesNot Available
Predicted Molecular Properties
PropertyValueSource
logP-0.28ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area34.14 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity2.89 m³·mol⁻¹ChemAxon
Polarizability1.53 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleNoChemAxon
Predicted Chromatographic Properties

Predicted Collision Cross Sections

PredictorAdduct TypeCCS Value (Å2)Reference
DeepCCS[M+H]+109.4230932474
DeepCCS[M-H]-107.69530932474
DeepCCS[M-2H]-142.83830932474
DeepCCS[M+Na]+116.16930932474

Predicted Kovats Retention Indices

Underivatized

MetaboliteSMILESKovats RI ValueColumn TypeReference
OxygenO=O577.3Standard polar33892256
OxygenO=O188.7Standard non polar33892256
OxygenO=O281.4Semi standard non polar33892256
Spectra

GC-MS Spectra

Spectrum TypeDescriptionSplash KeyDeposition DateSourceView
Predicted GC-MSPredicted GC-MS Spectrum - Oxygen GC-MS (Non-derivatized) - 70eV, Positivesplash10-001i-9000000000-2e78a9ed80eede2ed33a2016-09-22Wishart LabView Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - Oxygen GC-MS (Non-derivatized) - 70eV, PositiveNot Available2021-10-12Wishart LabView Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - Oxygen GC-MS (Non-derivatized) - 70eV, PositiveNot Available2021-10-12Wishart LabView Spectrum

MS/MS Spectra

Spectrum TypeDescriptionSplash KeyDeposition DateSourceView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 10V, Positive-QTOFsplash10-001i-9000000000-a9a93dd42f2cfa0b34c42015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 20V, Positive-QTOFsplash10-001i-9000000000-a9a93dd42f2cfa0b34c42015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 40V, Positive-QTOFsplash10-001i-9000000000-a9a93dd42f2cfa0b34c42015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 10V, Negative-QTOFsplash10-001i-9000000000-5e864878b295db1744732015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 20V, Negative-QTOFsplash10-001i-9000000000-5e864878b295db1744732015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 40V, Negative-QTOFsplash10-001i-9000000000-5e864878b295db1744732015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 10V, Positive-QTOFsplash10-001i-9000000000-9878c3ba827de483e23b2021-09-22Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 20V, Positive-QTOFsplash10-001i-9000000000-9878c3ba827de483e23b2021-09-22Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Oxygen 40V, Positive-QTOFsplash10-001i-9000000000-9878c3ba827de483e23b2021-09-22Wishart LabView Spectrum

IR Spectra

Spectrum TypeDescriptionDeposition DateSourceView
Predicted IR SpectrumIR Ion Spectrum (Predicted IRIS Spectrum, Adduct: [M+H]+)2023-02-03FELIX labView Spectrum
Predicted IR SpectrumIR Ion Spectrum (Predicted IRIS Spectrum, Adduct: [M+Na]+)2023-02-03FELIX labView Spectrum
Biological Properties
Cellular Locations
  • Extracellular
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Peroxisome
Biospecimen Locations
  • Blood
Tissue Locations
  • All Tissues
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
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 IDDB09140
Phenol Explorer Compound IDNot Available
FooDB IDFDB022589
KNApSAcK IDNot Available
Chemspider ID952
KEGG Compound IDC00007
BioCyc IDOXYGEN-MOLECULE
BiGG ID33493
Wikipedia LinkOxygen
METLIN ID3195
PubChem Compound977
PDB IDNot Available
ChEBI ID15379
Food Biomarker OntologyNot Available
VMH IDO2
MarkerDB IDNot Available
Good Scents IDNot Available
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
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  50. Cain SM, Curtis SE: Experimental models of pathologic oxygen supply dependency. Crit Care Med. 1991 May;19(5):603-12. [PubMed:2026022 ]
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  52. Edwards JD: Oxygen transport in cardiogenic and septic shock. Crit Care Med. 1991 May;19(5):658-63. [PubMed:2026028 ]
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  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 ]
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Only showing the first 10 proteins. There are 203 proteins in total.

Show all enzymes and transporters

Enzymes

Enzyme Details
1. Tyrosinase
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
Enzyme Details
2. Peroxisomal sarcosine oxidase
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 → 2,3,4,5-Tetrahydro-2-pyridinecarboxylic acid + Hydrogen peroxidedetails
Enzyme Details
3. Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
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
Enzyme Details
4. Aldehyde oxidase
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
Enzyme Details
5. Lathosterol oxidase
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
Enzyme Details
6. Dimethylaniline monooxygenase [N-oxide-forming] 5
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
Enzyme Details
7. Peroxisomal acyl-coenzyme A oxidase 1
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
Enzyme Details
8. D-aspartate oxidase
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
Enzyme Details
9. Heme oxygenase 2
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 + Iron + FAD + Waterdetails
Enzyme Details
10. Squalene monooxygenase
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 → (S)-2,3-Epoxysqualene + Acceptor + Waterdetails
Squalene + Oxygen + NADPH + Hydrogen Ion → (S)-2,3-Epoxysqualene + NADP + Waterdetails

Only showing the first 10 proteins. There are 203 proteins in total.

Show all enzymes and transporters