Cloned (Comment) | Organism |
---|---|
expression as a fusion product with the Escherichia coli maltose-binding protein | Pisum sativum |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pisum sativum | - |
- |
- |
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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
117 | - |
purified recombinant enzyme | Pisum sativum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ascorbate + H2O2 | - |
Pisum sativum | dehydroascorbate + H2O | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Pisum sativum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Pisum sativum |