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Literature summary for 1.11.1.7 extracted from

  • Spadiut, O.; Rossetti, L.; Dietzsch, C.; Herwig, C.
    Purification of a recombinant plant peroxidase produced in Pichia pastoris by a simple 2-step strategy (2012), Protein Expr. Purif., 86, 89-97.
    View publication on PubMed
Search for more literature for 1.11.1.7

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris strain CBS7435 Armoracia rusticana

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
 x * 60000, SDS-PAGE Armoracia rusticana

Organism

Organism UniProt Comment Textmining
Armoracia rusticana
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein recombinant enzyme produced in yeast is hyperglycosylated Armoracia rusticana

Purification (Commentary)

Purification (Comment) Organism
hydrophobic charge induction chromatography with 4-mercapto-ethyl-pyridine and Superdex 75 gel filtration Armoracia rusticana

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
-
 ?

Subunits

Subunits Comment Organism
? x * 60000, SDS-PAGE Armoracia rusticana

Synonyms

Synonyms Comment Organism
horseradish peroxidase
-
 Armoracia rusticana
HRP
-
 Armoracia rusticana

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 9 the enzyme shows high stability between pH 4.0 and 9.0. At lower and higher pH values a significant reduction of the enzymatic activity is observed Armoracia rusticana

Cofactor

Cofactor Comment Organism Structure
heme
-
 Armoracia rusticana

pI Value

Organism Comment pI Value Maximum pI Value
Armoracia rusticana calculated from amino acid sequence
-
 6.4