Saccharopepsin
Saccharopepsin (EC 3.4.23.25, yeast endopeptidase A, Saccharomyces aspartic proteinase, aspartic proteinase yscA, proteinase A, proteinase yscA, yeast proteinase A, Saccharomyces cerevisiae aspartic proteinase A, PRA) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-Val-Tyr bond in a synthetic substrate.
| Saccharopepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.25 | ||||||||
| CAS number | 37228-80-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme is present in baker's yeast (Saccharomyces cerevisiae).
References
- Hata T, Hayashi R, Dot E (1967). "Purification of yeast proteinases. Part III. Isolation and physicochemical properties of yeast proteinase A and C". Agric. Biol. Chem. 31: 357–367. doi:10.1080/00021369.1967.10858812.
- Meussdoerffer F, Tortora P, Holzer H (December 1980). "Purification and properties of proteinase A from yeast". The Journal of Biological Chemistry. 255 (24): 12087–93. PMID 7002931.
- Ammerer G, Hunter CP, Rothman JH, Saari GC, Valls LA, Stevens TH (July 1986). "PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors". Molecular and Cellular Biology. 6 (7): 2490–9. doi:10.1128/mcb.6.7.2490. PMC 367803. PMID 3023936.
External links
- Saccharopepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.