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Escherichia coli K-12 substr. MG1655 Compound: hydrogen peroxide

Synonyms: hydroperoxide, perhydrol, H2O2

Chemical Formula: H2O2

Molecular Weight: 34.015 Daltons

Monoisotopic Molecular Weight: 34.0054793084 Daltons

SMILES: OO

InChI: InChI=1S/H2O2/c1-2/h1-2H

InChIKey: InChIKey=MHAJPDPJQMAIIY-UHFFFAOYSA-N

Unification Links: CAS:7722-84-1 , ChEBI:16240 , ChemSpider:763 , HMDB:HMDB03125 , IAF1260:33570 , KEGG:C00027 , MetaboLights:MTBLC16240 , PubChem:784

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -32

Reactions known to consume the compound:

L-ascorbate degradation II (bacterial, aerobic) :
2 L-ascorbate + hydrogen peroxide + H+ → L-ascorbate + L-dehydro-ascorbate + 2 H2O

superoxide radicals degradation :
2 hydrogen peroxide → 2 H2O + oxygen

Not in pathways:
2 L-ascorbate + hydrogen peroxide + 2 H+ → 2 monodehydroascorbate radical + 2 H2O
hydrogen peroxide + Fe2+ → hydroxyl radical + Fe3+ + OH-
L-methionine + hydrogen peroxide → L-methionine S-oxide + H2O
hydrogen peroxide + a reduced electron acceptor → an oxidized electron acceptor + 2 H2O
hydrogen peroxide + 2 glutathione → glutathione disulfide + 2 H2O
a reduced thioredoxin + hydrogen peroxide → an oxidized thioredoxin + 2 H2O

Reactions known to produce the compound:

heme biosynthesis I (aerobic) , superpathway of heme biosynthesis from uroporphyrinogen-III :
protoporphyrinogen IX + 3 oxygen → protoporphyrin IX + 3 hydrogen peroxide

NAD biosynthesis I (from aspartate) :
L-aspartate + oxygen → hydrogen peroxide + α-iminosuccinate + H+

phenylethylamine degradation I :
2-phenylethylamine[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] → phenylacetaldehyde[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

putrescine degradation II :
γ-glutamyl-L-putrescine + H2O + oxygen → 4-(γ-glutamylamino)butanal + hydrogen peroxide + ammonium

pyridoxal 5'-phosphate biosynthesis I :
pyridoxine 5'-phosphate + oxygen → hydrogen peroxide + pyridoxal 5'-phosphate

pyridoxal 5'-phosphate salvage I :
pyridoxine 5'-phosphate + oxygen → hydrogen peroxide + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + oxygen + H2O → ammonium + hydrogen peroxide + pyridoxal 5'-phosphate

superoxide radicals degradation :
2 superoxide + 2 H+hydrogen peroxide + oxygen

threonine degradation III (to methylglyoxal) :
aminoacetone[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] → methylglyoxal[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

Not in pathways:
(S)-2-hydroxyglutarate + oxygen → 2-oxoglutarate + hydrogen peroxide
Cr6+ + 2 NAD(P)H + oxygen → Cr3+ + hydrogen peroxide + 2 NAD(P)+
N-methyl-L-tryptophan + oxygen + H2O → L-tryptophan + hydrogen peroxide + formaldehyde
a primary amine[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] → an aldehyde[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]
an aliphatic amine[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] → an aldehyde[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

In Reactions of unknown directionality:

Not in pathways:
2 Fe2+ + oxygen + 4 H2O = 2 [FeO(OH)] monomer + hydrogen peroxide + 4 H+
heme b + hydrogen peroxide = heme d
2 Fe2+ + hydrogen peroxide + 2 H2O = 2 [FeO(OH)] monomer + 4 H+
a phenolic donor + hydrogen peroxide = 2 a phenoxyl radical of a phenolic donor + 2 H2O

In Transport reactions:
hydrogen peroxide[periplasmic space]hydrogen peroxide[extracellular space]

Enzymes inhibited by hydrogen peroxide, sorted by the type of inhibition, are:

Inhibitor (Mechanism unknown) of: peptide deformylase [Anjem12] , cytosine deaminase [Anjem12] , superoxide dismutase [Hunter02] , glutathionylspermidine amidase [Chiang10]


References

Anjem12: Anjem A, Imlay JA (2012). "Mononuclear iron enzymes are primary targets of hydrogen peroxide stress." J Biol Chem 287(19);15544-56. PMID: 22411989

Chiang10: Chiang BY, Chen TC, Pai CH, Chou CC, Chen HH, Ko TP, Hsu WH, Chang CY, Wu WF, Wang AH, Lin CH (2010). "Protein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetASE/amidase in redox regulation." J Biol Chem 285(33);25345-53. PMID: 20530482

Hunter02: Hunter T, Bannister JV, Hunter GJ (2002). "Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue." Eur J Biochem 269(21);5137-48. PMID: 12392545


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC13A.