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Showing metabocard for Hydrogen peroxide (HMDB0003125)

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enzymes (53) Show 53 proteins
Record Information
Version5.0
StatusDetected and Quantified
Creation Date2006-05-22 15:12:34 UTC
Update Date2023-02-21 17:16:32 UTC
HMDB IDHMDB0003125
Secondary Accession Numbers
  • HMDB0006491
  • HMDB03125
  • HMDB06491
Metabolite Identification
Common NameHydrogen peroxide
DescriptionHydrogen peroxide (H2O2) is a very pale blue liquid that appears colourless in a dilute solution. H2O2 is slightly more viscous than water and is a weak acid. H2O2 is unstable and slowly decomposes in the presence of light. It has strong oxidizing properties and is, therefore, a powerful bleaching agent that is mostly used for bleaching paper. H2O2 has also found use as a disinfectant and as an oxidizer. H2O2 in the form of carbamide peroxide is widely used for tooth whitening (bleaching), both in professionally- and in self-administered products. H2O2 is a well-documented component of living cells and is a normal metabolite of oxygen in the aerobic metabolism of cells and tissues. A total of 31 human cellular H2O2 generating enzymes has been identified so far (PMID: 25843657 ). H2O2 plays important roles in host defence and oxidative biosynthetic reactions. At high levels (>100 nM) H2O2 is toxic to most cells due to its ability to non-specifically oxidize proteins, membranes and DNA, leading to general cellular damage and dysfunction. However, at low levels (<10 nM), H2O2 functions as a signalling agent, particularly in higher organisms. In plants, H2O2 plays a role in signalling to cause cell shape changes such as stomatal closure and root growth. As a messenger molecule in vertebrates, H2O2 diffuses through cells and tissues to initiate cell shape changes, to drive vascular remodelling, and to activate cell proliferation and recruitment of immune cells. H2O2 also plays a role in redox sensing, signalling, and redox regulation (PMID: 28110218 ). This is normally done through molecular redox “switches” such as thiol-containing proteins. The production and decomposition of H2O2 are tightly regulated (PMID: 17434122 ). In humans, H2O2 can be generated in response to various stimuli, including cytokines and growth factors. H2O2 is degraded by several enzymes including catalase and superoxide dismutase (SOD), both of which play important roles in keeping the amount of H2O2 in the body below toxic levels. H2O2 also appears to play a role in vitiligo. Vitiligo is a skin pigment disorder leading to patchy skin colour, especially among dark-skinned individuals. Patients with vitiligo have low catalase levels in their skin, leading to higher levels of H2O2. High levels of H2O2 damage the epidermal melanocytes, leading to a loss of pigment (PMID: 10393521 ). Accumulating evidence suggests that hydrogen peroxide H2O2 plays an important role in cancer development. Experimental data have shown that cancer cells produce high amounts of H2O2. An increase in the cellular levels of H2O2 has been linked to several key alterations in cancer, including DNA changes, cell proliferation, apoptosis resistance, metastasis, angiogenesis and hypoxia-inducible factor 1 (HIF-1) activation (PMID: 17150302 , 17335854 , 16677071 , 16607324 , 16514169 ). H2O2 is found in most cells, tissues, and biofluids. H2O2 levels in the urine can be significantly increased with the consumption of coffee and other polyphenolic-containing beverages (wine, tea) (PMID: 12419961 ). In particular, roasted coffee has high levels of 1,2,4-benzenetriol which can, on its own, lead to the production of H2O2. Normal levels of urinary H2O2 in non-coffee drinkers or fasted subjects are between 0.5-3 uM/mM creatinine whereas, for those who drink coffee, the levels are between 3-10 uM/mM creatinine (PMID: 12419961 ). It is thought that H2O2 in urine could act as an antibacterial agent and that H2O2 is involved in the regulation of glomerular function (PMID: 10766414 ).
Structure
Data?1676999792
MOL3D MOLSDF3D SDFPDB3D PDBSMILESInChI

MOL for HMDB0003125 (Hydrogen peroxide)

 
  Mrv1652309042000282D          
 
  2  1  0  0  0  0            999 V2000
   17.4487   -8.4975    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
   18.2737   -8.4975    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  1  0  0  0  0
M  END
Download

3D MOL for HMDB0003125 (Hydrogen peroxide)

HMDB0003125
     RDKit          3D
Hydrogen peroxide
  4  3  0  0  0  0  0  0  0  0999 V2000
   -0.6564   -0.4458   -0.1310 O   0  0  0  0  0  0  0  0  0  0  0  0
    0.6328   -0.4382    0.1346 O   0  0  0  0  0  0  0  0  0  0  0  0
   -1.0197    0.4546    0.0812 H   0  0  0  0  0  0  0  0  0  0  0  0
    1.0433    0.4295   -0.0847 H   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  1  0
  1  3  1  0
  2  4  1  0
M  END
Download

3D SDF for HMDB0003125 (Hydrogen peroxide)

 
  Mrv1652309042000282D          
 
  2  1  0  0  0  0            999 V2000
   17.4487   -8.4975    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
   18.2737   -8.4975    0.0000 O   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  1  0  0  0  0
M  END
> <DATABASE_ID>
HMDB0003125

> <DATABASE_NAME>
hmdb

> <SMILES>
OO

> <INCHI_IDENTIFIER>
InChI=1S/H2O2/c1-2/h1-2H

> <INCHI_KEY>
MHAJPDPJQMAIIY-UHFFFAOYSA-N

> <FORMULA>
H2O2

> <MOLECULAR_WEIGHT>
34.0147

> <EXACT_MASS>
34.005479308

> <JCHEM_ACCEPTOR_COUNT>
2

> <JCHEM_ATOM_COUNT>
4

> <JCHEM_AVERAGE_POLARIZABILITY>
2.291055697453342

> <JCHEM_BIOAVAILABILITY>
1

> <JCHEM_DONOR_COUNT>
2

> <JCHEM_FORMAL_CHARGE>
0

> <JCHEM_GHOSE_FILTER>
0

> <JCHEM_IUPAC>
peroxol

> <JCHEM_LOGP>
-0.447202414

> <JCHEM_MDDR_LIKE_RULE>
0

> <JCHEM_NUMBER_OF_RINGS>
0

> <JCHEM_PHYSIOLOGICAL_CHARGE>
0

> <JCHEM_PKA>
14.397218846455527

> <JCHEM_PKA_STRONGEST_ACIDIC>
11.520607090216412

> <JCHEM_PKA_STRONGEST_BASIC>
-4.189015938635916

> <JCHEM_POLAR_SURFACE_AREA>
40.46

> <JCHEM_REFRACTIVITY>
5.1292

> <JCHEM_ROTATABLE_BOND_COUNT>
0

> <JCHEM_RULE_OF_FIVE>
1

> <JCHEM_TRADITIONAL_IUPAC>
hydrogen peroxide

> <JCHEM_VEBER_RULE>
0

$$$$
Download

3D-SDF for HMDB0003125 (Hydrogen peroxide)

HMDB0003125
     RDKit          3D
Hydrogen peroxide
  4  3  0  0  0  0  0  0  0  0999 V2000
   -0.6564   -0.4458   -0.1310 O   0  0  0  0  0  0  0  0  0  0  0  0
    0.6328   -0.4382    0.1346 O   0  0  0  0  0  0  0  0  0  0  0  0
   -1.0197    0.4546    0.0812 H   0  0  0  0  0  0  0  0  0  0  0  0
    1.0433    0.4295   -0.0847 H   0  0  0  0  0  0  0  0  0  0  0  0
  1  2  1  0
  1  3  1  0
  2  4  1  0
M  END
Download

PDB for HMDB0003125 (Hydrogen peroxide)

HEADER    PROTEIN                                 04-SEP-20   NONE
TITLE     NULL                                                        
COMPND    MOLECULE:                                                   
SOURCE    NULL                                                        
KEYWDS    NULL                                                        
EXPDTA    NULL                                                        
AUTHOR    Marvin                                                      
REVDAT   1   04-SEP-20         0                                  
HETATM    1  O   UNK     0      32.571 -15.862   0.000  0.00  0.00           O+0
HETATM    2  O   UNK     0      34.111 -15.862   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 HMDB0003125 (Hydrogen peroxide)

COMPND    HMDB0003125
HETATM    1  O1  UNL     1      -0.656  -0.446  -0.131  1.00  0.00           O  
HETATM    2  O2  UNL     1       0.633  -0.438   0.135  1.00  0.00           O  
HETATM    3  H1  UNL     1      -1.020   0.455   0.081  1.00  0.00           H  
HETATM    4  H2  UNL     1       1.043   0.429  -0.085  1.00  0.00           H  
CONECT    1    2    3
CONECT    2    4
END
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SMILES for HMDB0003125 (Hydrogen peroxide)

OO
Download

INCHI for HMDB0003125 (Hydrogen peroxide)

InChI=1S/H2O2/c1-2/h1-2H
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View in JSmolView Stereo Labels
Synonyms
ValueSource
[OH(OH)]ChEBI
Dihydrogen dioxideChEBI
H2O2ChEBI
HOOHChEBI
OxydolChEBI
PerhydrolChEBI
OxyfullKegg
Adeka super elHMDB
AlboneHMDB
Albone 35HMDB
Albone DSHMDB
Anti-keim 50HMDB
AsepticperHMDB
BaquashockHMDB
CIXHMDB
Clarigel goldHMDB
Crestal whitestripsHMDB
CrystacideHMDB
DentaseptHMDB
Deslime LPHMDB
HioxylHMDB
HipoxHMDB
HybriteHMDB
Hydrogen dioxideHMDB
InhibineHMDB
Lase peroxideHMDB
Lensan aHMDB
Magic bleachingHMDB
MetrokurHMDB
MiraseptHMDB
Nite white excel 2HMDB
Odosat DHMDB
Opalescence xtraHMDB
OxigenalHMDB
OxyseptHMDB
Oxysept IHMDB
PegasylHMDB
PeroneHMDB
PeroxaanHMDB
PeroxcleanHMDB
Quasar briteHMDB
Select bleachHMDB
SuperoxolHMDB
T-StuffHMDB
Whiteness HPHMDB
WhitespeedHMDB
Xtra whiteHMDB
Hydrogen peroxide (H2O2)HMDB
HydroperoxideHMDB
Peroxide, hydrogenHMDB
Chemical FormulaH2O2
Average Molecular Weight34.0147
Monoisotopic Molecular Weight34.005479308
IUPAC Nameperoxol
Traditional Namehydrogen peroxide
CAS Registry Number7722-84-1
SMILES
OO
InChI Identifier
InChI=1S/H2O2/c1-2/h1-2H
InChI KeyMHAJPDPJQMAIIY-UHFFFAOYSA-N
Chemical Taxonomy
Description Belongs to the class of inorganic compounds known as homogeneous other non-metal compounds. These are inorganic non-metallic compounds in which the largest atom belongs to the class of 'other non-metals'.
KingdomInorganic compounds
Super ClassHomogeneous non-metal compounds
ClassHomogeneous other non-metal compounds
Sub ClassNot Available
Direct ParentHomogeneous other non-metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous other non metal
Molecular FrameworkNot Available
External Descriptors
Ontology
Not AvailableNot Available
Physical Properties
StateLiquid
Experimental Molecular Properties
PropertyValueReference
Melting Point-0.43 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility1000 mg/mL at 25 °CNot Available
LogPNot AvailableNot Available
Experimental Chromatographic PropertiesNot Available
Predicted Molecular Properties
PropertyValueSource
logP-0.45ChemAxon
pKa (Strongest Acidic)11.52ChemAxon
pKa (Strongest Basic)-4.2ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area40.46 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity5.13 m³·mol⁻¹ChemAxon
Polarizability2.29 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Predicted Chromatographic Properties

Predicted Collision Cross Sections

PredictorAdduct TypeCCS Value (Å2)Reference
DeepCCS[M+H]+109.47830932474
DeepCCS[M-H]-107.74730932474
DeepCCS[M-2H]-142.88630932474
DeepCCS[M+Na]+116.21230932474

Predicted Kovats Retention Indices

Underivatized

MetaboliteSMILESKovats RI ValueColumn TypeReference
Hydrogen peroxideOO1295.3Standard polar33892256
Hydrogen peroxideOO452.0Standard non polar33892256
Hydrogen peroxideOO382.3Semi standard non polar33892256
Spectra

GC-MS Spectra

Spectrum TypeDescriptionSplash KeyDeposition DateSourceView
Predicted GC-MSPredicted GC-MS Spectrum - Hydrogen peroxide GC-MS (Non-derivatized) - 70eV, Positivesplash10-001i-9000000000-4749d46780bc552fb9af2016-09-22Wishart LabView Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - Hydrogen peroxide GC-MS (Non-derivatized) - 70eV, PositiveNot Available2021-10-12Wishart LabView Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - Hydrogen peroxide 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 - Hydrogen peroxide 10V, Positive-QTOFsplash10-000i-9000000000-50a90bb1548c24e83fbe2015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 20V, Positive-QTOFsplash10-000i-9000000000-50a90bb1548c24e83fbe2015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 40V, Positive-QTOFsplash10-000i-9000000000-50a90bb1548c24e83fbe2015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 10V, Negative-QTOFsplash10-001i-9000000000-a9a93dd42f2cfa0b34c42015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 20V, Negative-QTOFsplash10-001i-9000000000-a9a93dd42f2cfa0b34c42015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 40V, Negative-QTOFsplash10-001i-9000000000-a9a93dd42f2cfa0b34c42015-09-15Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 10V, Negative-QTOFsplash10-001i-9000000000-d77c0031598ec85f72862021-09-22Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 20V, Negative-QTOFsplash10-001i-9000000000-d77c0031598ec85f72862021-09-22Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 40V, Negative-QTOFsplash10-001i-9000000000-d77c0031598ec85f72862021-09-22Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 10V, Positive-QTOFsplash10-000i-9000000000-86b45185e1deeaca15e12021-09-22Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 20V, Positive-QTOFsplash10-000i-9000000000-86b45185e1deeaca15e12021-09-22Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Hydrogen peroxide 40V, Positive-QTOFsplash10-000i-9000000000-86b45185e1deeaca15e12021-09-22Wishart 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+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 LocationsNot Available
Biospecimen Locations
  • Blood
  • Urine
Tissue LocationsNot Available
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified10.5 +/- 3.6 uMAdult (>18 years old)BothNormal details
UrineDetected and Quantified0.5-3 umol/mmol creatinineAdult (>18 years old)Not Specified
Normal		 details
UrineDetected and Quantified3-10 umol/mmol creatinineAdult (>18 years old)Not Specified
Normal		 details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified23.5 +/- 3.0 uMAdult (>18 years old)Both
Coronary heart disease		 details
BloodDetected and Quantified21.0 +/- 2.9 uMAdult (>18 years old)Both
Coronary heart disease		 details
BloodDetected and Quantified50.3 +/- 5.4 uMAdult (>18 years old)Both
Coronary heart disease		 details
BloodDetected and Quantified30.5 +/- 4.6 uMAdult (>18 years old)Both
Coronary heart disease		 details
Associated Disorders and Diseases
Disease References
Coronary heart disease
  1. Kazmierczak M, Wysocki H, Wykretowicz A, Minczykowski A: Estimation of hydrogen peroxide plasma levels in patients evaluated for coronary heart disease using dipyridamole infusion followed by SPECT. Coron Artery Dis. 1995 Jan;6(1):65-9. [PubMed:7767505 ]
Associated OMIM IDsNone
DrugBank IDDB11091
Phenol Explorer Compound IDNot Available
FooDB IDFDB014562
KNApSAcK IDNot Available
Chemspider ID763
KEGG Compound IDC00027
BioCyc IDHYDROGEN-PEROXIDE
BiGG ID33570
Wikipedia LinkHydrogen_peroxide
METLIN IDNot Available
PubChem Compound784
PDB IDNot Available
ChEBI ID16240
Food Biomarker OntologyNot Available
VMH IDH2O2
MarkerDB IDMDB00000411
Good Scents IDNot Available
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Lopez-Lazaro M: Dual role of hydrogen peroxide in cancer: possible relevance to cancer chemoprevention and therapy. Cancer Lett. 2007 Jul 8;252(1):1-8. Epub 2006 Dec 5. [PubMed:17150302 ]
  2. Schallreuter KU, Elwary S: Hydrogen peroxide regulates the cholinergic signal in a concentration dependent manner. Life Sci. 2007 May 30;80(24-25):2221-6. Epub 2007 Jan 25. [PubMed:17335854 ]
  3. Stone JR, Yang S: Hydrogen peroxide: a signaling messenger. Antioxid Redox Signal. 2006 Mar-Apr;8(3-4):243-70. [PubMed:16677071 ]
  4. Tredwin CJ, Naik S, Lewis NJ, Scully C: Hydrogen peroxide tooth-whitening (bleaching) products: review of adverse effects and safety issues. Br Dent J. 2006 Apr 8;200(7):371-6. [PubMed:16607324 ]
  5. Ardanaz N, Pagano PJ: Hydrogen peroxide as a paracrine vascular mediator: regulation and signaling leading to dysfunction. Exp Biol Med (Maywood). 2006 Mar;231(3):237-51. [PubMed:16514169 ]
  6. Go YM, Chandler JD, Jones DP: The cysteine proteome. Free Radic Biol Med. 2015 Jul;84:227-245. doi: 10.1016/j.freeradbiomed.2015.03.022. Epub 2015 Apr 3. [PubMed:25843657 ]
  7. Sies H: Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress. Redox Biol. 2017 Apr;11:613-619. doi: 10.1016/j.redox.2016.12.035. Epub 2017 Jan 5. [PubMed:28110218 ]
  8. Veal EA, Day AM, Morgan BA: Hydrogen peroxide sensing and signaling. Mol Cell. 2007 Apr 13;26(1):1-14. doi: 10.1016/j.molcel.2007.03.016. [PubMed:17434122 ]
  9. Schallreuter KU: Successful treatment of oxidative stress in vitiligo. Skin Pharmacol Appl Skin Physiol. 1999 May-Jun;12(3):132-8. doi: 10.1159/000029867. [PubMed:10393521 ]
  10. Hiramoto K, Kida T, Kikugawa K: Increased urinary hydrogen peroxide levels caused by coffee drinking. Biol Pharm Bull. 2002 Nov;25(11):1467-71. doi: 10.1248/bpb.25.1467. [PubMed:12419961 ]
  11. Long LH, Halliwell B: Coffee drinking increases levels of urinary hydrogen peroxide detected in healthy human volunteers. Free Radic Res. 2000 May;32(5):463-7. [PubMed:10766414 ]

Only showing the first 10 proteins. There are 53 proteins in total.

Show all enzymes and transporters

Enzymes

Enzyme Details
1. 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
2. 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
3. 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 → Nudifloramide + Hydrogen peroxide + Hydrogen Iondetails
Enzyme Details
4. 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
5. 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
6. Amine oxidase [flavin-containing] B
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
Enzyme Details
7. Amine oxidase [flavin-containing] A
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
Enzyme Details
8. Xanthine dehydrogenase/oxidase
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
Enzyme Details
9. Dihydroorotate dehydrogenase (quinone), mitochondrial
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
Enzyme Details
10. Peroxisomal acyl-coenzyme A oxidase 3
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

Only showing the first 10 proteins. There are 53 proteins in total.

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