Literature summary for 1.11.1.11 extracted from

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

Search for more literature for 1.11.1.11

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Pisum sativum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
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]

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

Substrates and Products (Substrate)

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Pisum sativum

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Release 2023.1 (January 2023)