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Literature summary for 1.11.1.7 extracted from

  • Guo, S.; Wang, L.; Lu, A.; Lu, T.; Ding, X.; Huang, X.
    Inhibition mechanism of lanthanum ion on the activity of horseradish peroxidase in vitro (2010), Spectrochim. Acta A. Mol. Biomol. Spectrosc., 75, 936-940.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
La3+ the formation of the La3+-HRP complex causes the destruction of the native structure of HRP molecule, leading to the decrease in the non-planarity of the porphyrin ring in the heme group of HRP molecule, and then in the exposure extent of active center, Fe(III) of the porphyrin ring of HRP molecule. Thus, the direct electrochemical and catalytic activities of HRP are decreased. When the molar ratio of La3+ and HRP is 10, the catalytic activity of HRP is decreased by 12% comparing with that of HRP in the absence of La3+ Armoracia rusticana

Organism

Organism UniProt Comment Textmining
Armoracia rusticana
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
horseradish peroxidase
-
Armoracia rusticana
HRP
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Armoracia rusticana

Cofactor

Cofactor Comment Organism Structure
heme
-
Armoracia rusticana