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Literature summary for 3.4.23.25 extracted from
- An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae (2002), Biochem. Biophys. Res. Commun., 295, 1020-1026.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | important in a number of pathological processes, including gastric ulcers, Alzheimer's disease, hypertension, malaria, and AIDS | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structures of the native enzyme solved by molecular replacement in monoclinic and trygonal crystal forms, trigonal space group P3(2)21, cell dimensions a = b = 84.6 A, c = 108.7 A, monoclinic space group P2(1), cell dimensions a = 82.97 A, b = 49.08 A, c = 94.69 A | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P07267 | yeast | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Aspartic proteinase | - |
Saccharomyces cerevisiae |
| Proteinase A | - |
Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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