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Literature summary 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

EC Number General Stability Organism
1.11.1.7 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

EC Number Inhibitors Comment Organism Structure
1.11.1.7 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.7 2.36
-
 4-Aminophenol native enzyme, at 30°C Armoracia rusticana
1.11.1.7 3.59
-
 phenol native enzyme, at 30°C Armoracia rusticana
1.11.1.7 18.76
-
 p-hydroxybenzoic acid native enzyme, at 30°C Armoracia rusticana

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.7 Armoracia rusticana
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.7 4-aminoantipyrin + H2O2
-
 Armoracia rusticana ?
-
 ?
1.11.1.7 4-aminophenol + H2O2
-
 Armoracia rusticana ?
-
 ?
1.11.1.7 p-hydroxybenzoic acid + H2O2
-
 Armoracia rusticana ?
-
 ?
1.11.1.7 phenol + H2O2
-
 Armoracia rusticana ?
-
 ?

Synonyms

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.11.1.7 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.7 311.7
-
 p-hydroxybenzoic acid native enzyme, at 30°C Armoracia rusticana
1.11.1.7 691.7
-
 phenol native enzyme, at 30°C Armoracia rusticana
1.11.1.7 1272
-
 4-Aminophenol native enzyme, at 30°C Armoracia rusticana

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.7 heme
-
 Armoracia rusticana