Saccharopepsin
| 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 | ||||||||
| |||||||||
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.
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. (1980). "Purification and properties of proteinase A from yeast". J. Biol. Chem. 255: 12087–12093. PMID 7002931.
- ↑ Ammerer, G.; Hunter, C.P.; Rothman, J.H.; Saari, G.C.; Valls, L.A.; Stevens, T.H. (1987). "PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors". Mol. Cell. Biol. 6: 2490–2499. PMID 3023936.
External links
- Saccharopepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
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