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Literature summary for 1.11.1.11 extracted from

  • Badyal, S.K.; Metcalfe, C.L.; Basran, J.; Efimov, I.; Moody, P.C.; Raven, E.L.
    Iron oxidation state modulates active site structure in a heme peroxidase (2008), Biochemistry, 47, 4403-4409.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
W41A the mutant is a six-coordinate heme peroxidase which has bis-histidine coordination, like a cytochrome, but that is catalytically active because the distal histidine reversibly dissociates to form a five-coordinate heme in response to binding of hydrogen peroxide Glycine max

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Glycine max 5829
-

Organism

Organism UniProt Comment Textmining
Glycine max Q43758
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ascorbate + H2O2
-
Glycine max dehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
APX
-
Glycine max
ascorbate peroxidase
-
Glycine max

Cofactor

Cofactor Comment Organism Structure
heme
-
Glycine max