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Literature summary for 3.2.1.171 extracted from
- Crystallization and preliminary X-ray studies of rhamnogalacturonase A from Aspergillus aculeatus (1997), Acta Crystallogr. Sect. D, 53, 105-107.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapour-diffusion technique, crystals diffract beyond 2.0 A resolution and belong to one of the orthorhombic space groups 12(1)2(1)2 or I222, with the unit-cell parameters a = 62.9, b = 125.4 and c = 137.0 A | Aspergillus aculeatus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50100 | - |
x * 50100, MALDI-TOF analysis | Aspergillus aculeatus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus aculeatus | Q00001 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme is highly glycosylated corresponding to 5.9 kDa | Aspergillus aculeatus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 50100, MALDI-TOF analysis | Aspergillus aculeatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| rhamnogalacturonase A | - |
Aspergillus aculeatus |
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