Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.11 extracted from

  • Sano, S.; Ueda, M.; Kitajima, S.; Takeda, T.; Shigeoka, S.; Kurano, N.; Miyachi, S.; Miyake, C.; Yokota, A.
    Characterization of ascorbate peroxidases from unicellular red alga Galdieria partita (2001), Plant Cell Physiol., 42, 433-440.
    View publication on PubMed
Search for more literature for 1.11.1.11

Inhibitors

Inhibitors Comment Organism Structure
KCN
-
 Galdieria partita
NaN3
-
 Galdieria partita

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km values comparable with those of higher plants Galdieria partita

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 both enzymes A and B Galdieria partita

Organism

Organism UniProt Comment Textmining
Galdieria partita
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using hydrophobic chromatography, separation of two isozymes: enzyme-A and enzyme-B, enzyme-B accounts for 85% of the total activity, purification of both enzymes Galdieria partita

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ascorbate + H2O2
-
 Galdieria partita dehydroascorbate + H2O
-
 ?
L-ascorbic acid + tert-butylhydroperoxide both enzymes A and B Galdieria partita dehydroascorbate + tert-butylalcohol
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 28000, both enzymes A and B Galdieria partita

Cofactor

Cofactor Comment Organism Structure
heme
-
 Galdieria partita