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Literature summary for 1.11.1.11 extracted from

  • Metcalfe, C.L.; Ott, M.; Patel, N.; Singh, K.; Mistry, S.C.; Goff, H.M.; Raven, E.L.
    Autocatalytic formation of green heme: evidence for H2O2-dependent formation of a covalent methionine-heme linkage in ascorbate peroxidase (2004), J. Am. Chem. Soc., 126, 16242-16248.
    View publication on PubMed
Search for more literature for 1.11.1.11

Protein Variants

Protein Variants Comment Organism
S160M expression of apo-protein in Escherichia coli, reconstitution with exogenous heme, gives kinetic properties similar to wild-type enzyme Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.102
-
 L-ascorbate mutant S160M, pH 7.0, 25°C Pisum sativum
0.355
-
 L-ascorbate wild-type, pH 7.0, 25°C Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Pisum sativum 5829
-

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
 recombinant enzyme
-

Reaction

Reaction Comment Organism Reaction ID
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O mechanism Pisum sativum
a

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
156
-
 L-ascorbate mutant S160M, pH 7.0, 25°C Pisum sativum
159
-
 L-ascorbate wild-type, pH 7.0, 25°C Pisum sativum