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Literature summary for 1.11.1.7 extracted from

  • Feng, J.Y.; Liu, J.Z.; Ji, L.N.
    Thermostability, solvent tolerance, catalytic activity and conformation of cofactor modified horseradish peroxidase (2008), Biochimie, 90, 1337-1346.
    View publication on PubMed

General Stability

General Stability Organism
cofactor modification(heminD1 in rHRP1 and heminD2 in rHRP2 instead of heme) increases the substrate affinity and catalytic efficiency both in aqueous buffer and some organic solvents, the catalytic efficiency for phenol oxidation is increased by about 55% for rHRP1 in aqueous buffer, and it is also increased by about 70% for rHRP1 in 10% (v/v) acetonitrile. Armoracia rusticana

Inhibitors

Inhibitors Comment Organism Structure
acetonitrile about 98% activity is lost for native HRP after incubation in 50% (v/v) acetonitrile at 35°C for 3 h, native HRP only possess less than 20% activity in 30% (v/v) acetonitrile Armoracia rusticana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.36
-
4-Aminophenol native enzyme, at 30°C Armoracia rusticana
3.59
-
phenol native enzyme, at 30°C Armoracia rusticana
18.76
-
p-hydroxybenzoic acid native enzyme, at 30°C Armoracia rusticana

Organism

Organism UniProt Comment Textmining
Armoracia rusticana
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminoantipyrin + H2O2
-
Armoracia rusticana ?
-
?
4-aminophenol + H2O2
-
Armoracia rusticana ?
-
?
p-hydroxybenzoic acid + H2O2
-
Armoracia rusticana ?
-
?
phenol + H2O2
-
Armoracia rusticana ?
-
?

Synonyms

Synonyms Comment Organism
horseradish peroxidase C
-
Armoracia rusticana
HRP
-
Armoracia rusticana
rHRP1 apo-horseradish peroxidase constituted with the artificial prostethic group heminD1 Armoracia rusticana
rHRP2 apo-horseradish peroxidase constituted with the artificial prostethic group heminD2 Armoracia rusticana

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65 76.5 the melting temperature is at 70°C for the native enzyme and at 75.4°C for the cofactor-modified enzyme rHRP1 and at 76.5°C for the cofactor-modified enzyme rHRP2. the reconstituted HRPs with modified hemin show higher thermostability in aqueous buffer. After the exposure for 1.5 h at 65°C, native HRP retains only about 15% activity, the reconstituted HRPs, however, retained about 60% activity Armoracia rusticana

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
311.7
-
p-hydroxybenzoic acid native enzyme, at 30°C Armoracia rusticana
691.7
-
phenol native enzyme, at 30°C Armoracia rusticana
1272
-
4-Aminophenol native enzyme, at 30°C Armoracia rusticana

Cofactor

Cofactor Comment Organism Structure
heme
-
Armoracia rusticana