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Literature summary for 3.4.23.4 extracted from
- Characterization of Mucor pusillus rennin expressed in Pichia pastoris: enzymic, spectroscopic and calorimetric studies (2000), Biotechnol. Appl. Biochem., 31, 77-84.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Pichia pastoris | Rhizomucor pusillus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 44000 | - |
x * 44000, SDS-PAGE | Rhizomucor pusillus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhizomucor pusillus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | 12% glycosylated, oligomannoside attached covalently | Rhizomucor pusillus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Rhizomucor pusillus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 44000, SDS-PAGE | Rhizomucor pusillus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme undergoes irreversible, highly scan-rate-dependent thermal denaturation under all the experimental conditions investigated (pH 2-12, 20-50°C). Between pH 3.0 and 7.0, only one endotherm characterizes the thermal denaturation of the enzyme. Upon reaching pH 7.5, the denaturation is characterized by two endotherms | Rhizomucor pusillus |
| 25 | - |
most stable at pH 5.0, denaturation can be fitted to the two-state irreversible model | Rhizomucor pusillus |
| 65 | - |
transition midpoint | Rhizomucor pusillus |
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Release 2023.1 (January 2023)
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