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Literature summary for 3.2.1.171 extracted from
- Kauppinen, S.; Christgau, S.; Andersen, L.N.; Heldt-Hansen, H.P.; Dörreich, K.; Dalboge, H.: Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus (1994), J. Biol. Chem., 269, 29182-29189.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Aspergillus oryzae | Aspergillus aculeatus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 44162 | - |
x * 44162, calculated from sequence | Aspergillus aculeatus |
| 59000 | - |
x * 59000, native enzyme | Aspergillus aculeatus |
| 62000 | - |
x * 62000, recombinant enzyme, SDS-PAGE | Aspergillus aculeatus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus aculeatus | Q00001 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | a significant amount of glycan structures is attached to the enzyme. Three potential sites for N-linked glycosylation are present in the primary structure of RGase A (amino acid positions 50, 235, and 317). Recombinant RGase A is overglycosylated by approximately 3 kDa compared with native RGase A | Aspergillus aculeatus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| azurine dyed and cross-linked galactan + H2O | - |
Aspergillus aculeatus | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 44162, calculated from sequence | Aspergillus aculeatus |
| ? | x * 59000, native enzyme | Aspergillus aculeatus |
| ? | x * 62000, recombinant enzyme, SDS-PAGE | Aspergillus aculeatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RGase A | - |
Aspergillus aculeatus |
| rhamnogalacturonase A | - |
Aspergillus aculeatus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
rRGase A has no distinct temperature optimum from 30 to 50°C | Aspergillus aculeatus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
2 h, enzyme retains 70% of its activity | Aspergillus aculeatus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | - |
- |
Aspergillus aculeatus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
unstable above | Aspergillus aculeatus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Aspergillus aculeatus | calculated from sequence | - |
4.3 |
| Aspergillus aculeatus | isoelectric focusing | - |
4.5 |
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