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

BRENDA support

Literature summary extracted from

  • Patterson, W.R.; Poulos, T.L.
    Characterization and Crystallization of Recombinant Pea Cytosolic Ascorbate Peroxidase (1994), J. Biol. Chem., 269, 17020-17024.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.11 expression as a fusion product with the Escherichia coli maltose-binding protein Pisum sativum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.11 of the recombinant enzyme, using the hanging drop, vapor diffusion method, the recombinant enzyme forms monoclinic crystals in space group C2 with a: 132.80 A, b: 53.26 A, c: 171.96 A and beta: 106.93° Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.11 Pisum sativum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.11 of the recombinant enzyme, using affinity chromatography on amylose colum, and column chromatography on hydroxylapatite and FFQ-Sepharose Pisum sativum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.11 117
-
 purified recombinant enzyme Pisum sativum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.11 L-ascorbate + H2O2
-
 Pisum sativum dehydroascorbate + H2O
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.11 7
-
 assay at Pisum sativum

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.11 heme
-
 Pisum sativum