Yapsin 1
| Yapsin 1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.41 | ||||||||
| CAS number | 205132-58-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Yapsin 1 (EC 3.4.23.41, yeast aspartic protease 3, Yap3 gene product (Saccharomyces cerevisiae)) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
This enzyme belongs to the peptidase family A1 of pepsin.
References
- ↑ Cawley, N.X.; Chen, H.C.; Beinfeld, M.C.; Loh, Y.P. (1996). "Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3". J. Biol. Chem. 271: 4168–4176. doi:10.1074/jbc.271.8.4168. PMID 8626758.
- ↑ Fuller, R.S.; Rawlings, N.D.; Woessner, J.F. (1998). "Yapsin 2". In Barrett, A.J. Handbook of Proteolytic Enzymes. London: Academic Press. pp. 908–909.
- ↑ Olsen, V.; Guruprasad, K.; Cawley, N.X.; Chen, H.C.; Blundell, T.L.; Loh, Y.P. (1998). "Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p) enhanced for substrates with arginine residues flanking the P1 site: correlation with electronegative active-site pockets predicted by molecular modeling". Biochemistry. 37: 2768–2777. doi:10.1021/bi9724826. PMID 9485427.
External links
- Yapsin+1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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