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Identification
YMDB IDYMDB00888
NameHydrogen peroxide
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionHydrogen peroxide, also known as albone or dihydrogen dioxide, 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'. Hydrogen peroxide is an extremely weak basic (essentially neutral) compound (based on its pKa). Hydrogen peroxide exists in all living species, ranging from bacteria to humans.
Structure
Thumb
Synonyms
  • Hydrogen dioxide
  • [OH(OH)]
  • Dihydrogen dioxide
  • H2O2
  • HOOH
  • Oxydol
  • Perhydrol
  • Oxyfull
  • Adeka super el
  • Albone
  • Albone 35
  • Albone DS
  • Anti-keim 50
  • Asepticper
  • Baquashock
  • CIX
  • Clarigel gold
  • Crestal whitestrips
  • Crystacide
  • Dentasept
  • Deslime LP
  • Hioxyl
  • Hipox
  • Hybrite
  • Inhibine
  • Lase peroxide
  • Lensan a
  • Magic bleaching
  • Metrokur
  • Mirasept
  • Nite white excel 2
  • Odosat D
  • Opalescence xtra
  • Oxigenal
  • Oxysept
  • Oxysept I
  • Pegasyl
  • Perone
  • Peroxaan
  • Peroxclean
  • Quasar brite
  • Select bleach
  • Superoxol
  • T-Stuff
  • Whiteness HP
  • Whitespeed
  • Xtra white
  • Hydrogen peroxide (H2O2)
  • Hydroperoxide
  • Peroxide, hydrogen
CAS number7722-84-1
WeightAverage: 34.0147
Monoisotopic: 34.005479308
InChI KeyMHAJPDPJQMAIIY-UHFFFAOYSA-N
InChIInChI=1S/H2O2/c1-2/h1-2H
IUPAC Nameperoxol
Traditional IUPAC Namehydrogen peroxide
Chemical FormulaH2O2
SMILES[H]OO[H]
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
Physical Properties
StateLiquid
Charge0
Melting point-0.43 °C
Experimental Properties
PropertyValueReference
Water Solubility1000 mg/mL at 25 oC [RADDING,SB et al. (1977)]PhysProp
LogPNot AvailablePhysProp
Predicted 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
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • mitochondrion
  • nucleus
  • peroxisome
  • cytoplasm
Organoleptic Properties
Flavour/OdourSource
BitterFDB014562
SMPDB Pathways
Porphyrin MetabolismPW002462 ThumbThumb?image type=greyscaleThumb?image type=simple
Vitamin B6PW002488 ThumbThumb?image type=greyscaleThumb?image type=simple
beta-Alanine metabolismPW002381 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
beta-Alanine metabolismec00410 Map00410
SMPDB Reactions
L-Aspartic acid + water + oxygenOxalacetic acid + Ammonia + Hydrogen peroxide
Spermine + water + oxygenHydrogen peroxide + 3-Aminopropionaldehyde + Spermidine
Protoporphyrinogen IX + oxygenProtoporphyrin IX + Hydrogen peroxide
Pyridoxine 5'-phosphate + oxygenPyridoxal 5'-phosphate + Hydrogen peroxide
Pyridoxamine 5'-phosphate + oxygen + waterPyridoxal 5'-phosphate + Hydrogen peroxide + Ammonium
KEGG Reactions
decanoyl-CoA + oxygenHydrogen peroxide + trans-dec-2-enoyl-CoA
lauroyl-CoA + oxygen(2E)-Dodecenoyl-CoA + Hydrogen peroxide
oxygen + hexacosanoyl-CoAHydrogen peroxide + trans-hexacos-2-enoyl-CoA
Palmityl-CoA + oxygenHydrogen peroxide + hexadec-2-enoyl-CoA
stearoyl-CoA + oxygentrans-octadec-2-enoyl-CoA + Hydrogen peroxide
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-001i-9000000000-4749d46780bc552fb9afJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-9000000000-50a90bb1548c24e83fbeJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-9000000000-50a90bb1548c24e83fbeJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-9000000000-50a90bb1548c24e83fbeJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-001i-9000000000-a9a93dd42f2cfa0b34c4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-9000000000-a9a93dd42f2cfa0b34c4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-001i-9000000000-a9a93dd42f2cfa0b34c4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-001i-9000000000-d77c0031598ec85f7286JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-9000000000-d77c0031598ec85f7286JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-001i-9000000000-d77c0031598ec85f7286JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-9000000000-86b45185e1deeaca15e1JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-9000000000-86b45185e1deeaca15e1JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-9000000000-86b45185e1deeaca15e1JSpectraViewer
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Verduyn, C., Giuseppin, M. L., Scheffers, W. A., van Dijken, J. P. (1988). "Hydrogen peroxide metabolism in yeasts." Appl Environ Microbiol 54:2086-2090.16347719
  • Hiltunen, J. K., Mursula, A. M., Rottensteiner, H., Wierenga, R. K., Kastaniotis, A. J., Gurvitz, A. (2003). "The biochemistry of peroxisomal beta-oxidation in the yeast Saccharomyces cerevisiae." FEMS Microbiol Rev 27:35-64.12697341
  • Geisbrecht, B. V., Zhu, D., Schulz, K., Nau, K., Morrell, J. C., Geraghty, M., Schulz, H., Erdmann, R., Gould, S. J. (1998). "Molecular characterization of Saccharomyces cerevisiae Delta3, Delta2-enoyl-CoA isomerase." J Biol Chem 273:33184-33191.9837886
  • Lee, B. H., Huh, W. K., Kim, S. T., Lee, J. S., Kang, S. O. (1999). "Bacterial production of D-erythroascorbic acid and L-ascorbic acid through functional expression of Saccharomyces cerevisiae D-arabinono-1,4-lactone oxidase in Escherichia coli." Appl Environ Microbiol 65:4685-4687.10508108
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID16240
HMDB IDHMDB03125
Pubchem Compound ID784
Kegg IDC00027
ChemSpider ID763
FOODB IDFDB014562
WikipediaHydrogen peroxide
BioCyc IDHYDROGEN-PEROXIDE

Enzymes

General function:
Involved in glutathione peroxidase activity
Specific function:
May constitute a glutathione peroxidase-like protective system against oxidative stresses
Gene Name:
GPX2
Uniprot ID:
P38143
Molecular weight:
18406.0
Reactions
2 glutathione + H(2)O(2) → glutathione disulfide + 2 H(2)O.
2 glutathione + a lipid hydroperoxide → glutathione disulfide + lipid + H2O
General function:
Involved in D-arabinono-1,4-lactone oxidase activity
Specific function:
Can oxidize L-gulono-1,4-lactone as well as D-arabinono- 1,4-lactone and L-galactono-1,4-lactone
Gene Name:
ALO1
Uniprot ID:
P54783
Molecular weight:
59493.19922
Reactions
D-arabinono-1,4-lactone + O(2) → dehydro-D-arabinono-1,4-lactone + H(2)O(2).
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:
PDX3
Uniprot ID:
P38075
Molecular weight:
26908.0
Reactions
Pyridoxamine 5'-phosphate + H(2)O + O(2) → pyridoxal 5'-phosphate + NH(3) + H(2)O(2).
Pyridoxine 5'-phosphate + O(2) → pyridoxal 5'-phosphate + H(2)O(2).
General function:
Amino acid transport and metabolism
Specific function:
Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance
Gene Name:
FMS1
Uniprot ID:
P50264
Molecular weight:
57805.10156
Reactions
Spermine + O(2) + H(2)O → spermidine + 3-aminopropanal + H(2)O(2).
Spermidine + O(2) + H(2)O → putrescine + 3-aminopropanal + H(2)O(2).
N(1)-acetylspermine + O(2) + H(2)O → spermidine + 3-acetamidopropanal + H(2)O(2).
N(1)-acetylspermidine + O(2) + H(2)O → putrescine + 3-acetamidopropanal + H(2)O(2).
N(8)-acetylspermidine + O(2) + H(2)O → 4-acetamidobutanal + trimethylenediamine + H(2)O(2).
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)
Gene Name:
POX1
Uniprot ID:
P13711
Molecular weight:
84041.39844
Reactions
Acyl-CoA + O(2) → trans-2,3-dehydroacyl-CoA + H(2)O(2).
General function:
Involved in glutathione peroxidase activity
Specific function:
May constitute a glutathione peroxidase-like protective system against oxidative stresses
Gene Name:
GPX1
Uniprot ID:
P36014
Molecular weight:
19484.5
Reactions
2 glutathione + H(2)O(2) → glutathione disulfide + 2 H(2)O.
2 glutathione + a lipid hydroperoxide → glutathione disulfide + lipid + H2O
General function:
Involved in oxygen-dependent protoporphyrinogen oxidase activity
Specific function:
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX
Gene Name:
HEM14
Uniprot ID:
P40012
Molecular weight:
59702.39844
Reactions
Protoporphyrinogen-IX + 3 O(2) → protoporphyrin-IX + 3 H(2)O(2).
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:
HEM13
Uniprot ID:
P11353
Molecular weight:
37711.30078
Reactions
Coproporphyrinogen-III + O(2) + 2 H(+) → protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O.
General function:
Involved in electron carrier activity
Specific function:
Could be a fumarate reductase
Gene Name:
OSM1
Uniprot ID:
P21375
Molecular weight:
55064.80078
Reactions
General function:
Involved in electron carrier activity
Specific function:
Monothiol glutaredoxin involved in iron-sulfur biogenesis. Required for normal iron homeostasis. Protects cells against oxidative damage due to reactive oxygen species
Gene Name:
GRX5
Uniprot ID:
Q02784
Molecular weight:
16931.30078
Reactions
General function:
Involved in glutathione peroxidase activity
Specific function:
Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYP1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYP1 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598') and a reduced Cys-36 in HYP1/GPX3
Gene Name:
HYR1
Uniprot ID:
P40581
Molecular weight:
18641.40039
Reactions
2 R'-SH + ROOH → R'-S-S-R' + H(2)O + ROH.
2 glutathione + a lipid hydroperoxide → glutathione disulfide + lipid + H2O
General function:
Involved in electron carrier activity
Specific function:
Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S- transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage
Gene Name:
GRX2
Uniprot ID:
P17695
Molecular weight:
15861.2998
Reactions
General function:
Involved in electron carrier activity
Specific function:
Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S- transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage
Gene Name:
GRX1
Uniprot ID:
P25373
Molecular weight:
12380.09961
Reactions
General function:
Involved in electron carrier activity
Specific function:
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl- hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER- derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress
Gene Name:
TRX2
Uniprot ID:
P22803
Molecular weight:
11203.7998
Reactions
General function:
Involved in electron carrier activity
Specific function:
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl- hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER- derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism
Gene Name:
TRX1
Uniprot ID:
P22217
Molecular weight:
11234.90039
Reactions
General function:
Involved in metal ion binding
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Gene Name:
SOD1
Uniprot ID:
P00445
Molecular weight:
15854.59961
Reactions
2 superoxide + 2 H(+) → O(2) + H(2)O(2).
General function:
Involved in superoxide dismutase activity
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Gene Name:
SOD2
Uniprot ID:
P00447
Molecular weight:
25774.09961
Reactions
2 superoxide + 2 H(+) → O(2) + H(2)O(2).
General function:
Involved in catalytic activity
Specific function:
In the de novo pyrimidine biosynthesic pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate and the reduction of fumarate to succinate. Does not use oxaloacetate and NAD or NADP as electron acceptors
Gene Name:
URA1
Uniprot ID:
P28272
Molecular weight:
34800.60156
Reactions
(S)-dihydroorotate + O(2) → orotate + H(2)O(2).
(S)-dihydroorotate + a quinone → orotate + a quinol
General function:
Involved in iron ion binding
Specific function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain
Gene Name:
CYC1
Uniprot ID:
P00044
Molecular weight:
12181.90039
Reactions
General function:
Involved in iron ion binding
Specific function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain
Gene Name:
CYC7
Uniprot ID:
P00045
Molecular weight:
12532.2998
Reactions
General function:
Involved in electron carrier activity
Specific function:
Not Available
Gene Name:
TRX3
Uniprot ID:
P25372
Molecular weight:
14432.0
General function:
Involved in catalase activity
Specific function:
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide
Gene Name:
CTT1
Uniprot ID:
P06115
Molecular weight:
64583.0
Reactions
2 H(2)O(2) → O(2) + 2 H(2)O.
General function:
Involved in catalase activity
Specific function:
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide
Gene Name:
CTA1
Uniprot ID:
P15202
Molecular weight:
58555.19922
Reactions
2 H(2)O(2) → O(2) + 2 H(2)O.
General function:
Involved in peroxidase activity
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Gene Name:
CCP1
Uniprot ID:
P00431
Molecular weight:
40352.69922
Reactions
2 ferrocytochrome c + H(2)O(2) → 2 ferricytochrome c + 2 H(2)O.
General function:
Involved in thiol oxidase activity
Specific function:
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1
Gene Name:
ERV2
Uniprot ID:
Q12284
Molecular weight:
22141.30078
Reactions
4 R'C(R)SH + O(2) → 2 R'C(R)S-S(R)CR' + 2 H(2)O.
General function:
Involved in thiol oxidase activity
Specific function:
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins
Gene Name:
ERV1
Uniprot ID:
P27882
Molecular weight:
21639.30078
Reactions
4 R'C(R)SH + O(2) → 2 R'C(R)S-S(R)CR' + 2 H(2)O.