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Literature summary for 1.11.1.11 extracted from

  • Kitajima, S.; Shimaoka, T.; Kurioka, M.; Yokota, A.
    Irreversible cross-linking of heme to the distal tryptophan of stromal ascorbate peroxidase in response to rapid inactivation by H2O2 (2007), FEBS J., 274, 3013-3020.
    View publication on PubMed
Search for more literature for 1.11.1.11

Protein Variants

Protein Variants Comment Organism
W35F mutation does not cause a significant change in the structure of tsAPX. Mutation increases H2O2 tolerance. 2.3fold decrease in KM-value for L-ascorbate. 4.3fold increase in Km-value for H2O2 Nicotiana tabacum

Inhibitors

Inhibitors Comment Organism Structure
H2O2 when inactivated by H2O2, heme is irreversibly cross-linked to the APX apoprotein. tsAPXW35F is inactivated in 3 min by H2O2. It is possible that tsAPXW35F is inactivated by adistinct mechanism because the heme can no longer be cross-linked to the enzyme Nicotiana tabacum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0217
-
 H2O2 wild-type enzyme Nicotiana tabacum
0.0939
-
 H2O2 mutant enzyme W35F Nicotiana tabacum
0.17
-
 L-ascorbate mutant enzyme W35F Nicotiana tabacum
0.395
-
 L-ascorbate wild-type enzyme Nicotiana tabacum

Organism

Organism UniProt Comment Textmining
Nicotiana tabacum Q9TNL9
-
-

Substrates and Products (Substrate)

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