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Literature summary for 5.3.4.1 extracted from
- Biochemical and biophysical characterization of a novel plant protein disulfide isomerase (2009), Biopolymers, 92, 35-43.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 56000 | - |
and dimer. 1 * 62000, gel filtration, 1 * 56000, calculated | Oldenlandia affinis |
| 56000 | - |
and monomer. 2 * 62000, gel filtration, 2 * 56000, calculated | Oldenlandia affinis |
| 56000 | - |
x * 62000, gel filtration, x * 56000, calculated | Oldenlandia affinis |
| 62000 | - |
gel filtration | Oldenlandia affinis |
| 122000 | - |
gel filtration | Oldenlandia affinis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oldenlandia affinis | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | and monomer. 2 * 62000, gel filtration, 2 * 56000, calculated | Oldenlandia affinis |
| monomer | and dimer. 1 * 62000, gel filtration, 1 * 56000, calculated | Oldenlandia affinis |
| More | in solution at low concentration, enzyme comprises mainly monomers. At increasing concentrations, fractions of dimers and higher order oligomers are observed. Oligomerization is not driven by formation of intermolecular disulfide bonds, but by non-covalent interactions | Oldenlandia affinis |
| oligomer | x * 62000, gel filtration, x * 56000, calculated | Oldenlandia affinis |
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