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Literature summary for 1.11.1.7 extracted from

  • Howes, B.D.; Brissett, N.C.; Doyle, W.A.; Smith, A.T.; Smulevich, G.
    Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S. Evidence for selective effects on the reduced state of the enzyme (2005), FEBS J., 272, 5514-5521.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of Thr171Ser mutant enzyme in Escherichia coli Armoracia rusticana

Protein Variants

Protein Variants Comment Organism
T171S loss of a structural restraint in the proximal heme pocket that allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein. Significant change in the Fe2+/Fe3+ redox potential of the mutant T171S Armoracia rusticana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
607
-
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) 25°C, pH 5.0, mutant enzyme Armoracia rusticana

Organism

Organism UniProt Comment Textmining
Armoracia rusticana P00433
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
-
Armoracia rusticana oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
?

Cofactor

Cofactor Comment Organism Structure
heme loss of a structural restraint in the proximal heme pocket of mutant enzyme T171S allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein Armoracia rusticana