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DeutschSaccharopepsin
| Saccharopepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.25 | ||||||||
| CAS no. | 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).
Proteinase A is an aspartic proteinase found in Saccharomyces cerevisiae, commonly called “Brewer’s Yeast” or “Baker’s Yeast” and is used in the fermentation processes of beer and wine making. Fermentation can cause stress conditions for Saccharomyces cerevisiae and proteinase A can be excreted from the cell.[4]
Structure
Proteinase A is relatively simple protein and is 329 amino acid residues in length. It is composed of both alpha helices and beta pleated sheets, with beta pleated sheets being the prevailing structure.[5]
Proteinase A has two symmetrical lobes. The lobes are folded so that an aspartic acid from each lobe line up to form the active site of the protein. The structure of proteinase A is stabilized by two separate disulfide bridges, one in each lobe. The structure also includes a malleable sheet composed of beta pleated sheets that can cover and uncover the active site.[4]
- ^ 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. doi:10.1016/S0021-9258(19)70248-8. 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.
- ^ a b c Song, Lulu; Chen, Yefu; Du, Yongjing; Wang, Xibin; Guo, Xuewu; Dong, Jian; Xiao, Dongguang (November 2017). "Saccharomyces cerevisiae proteinase A excretion and wine making". World Journal of Microbiology and Biotechnology. 33 (11): 210. doi:10.1007/s11274-017-2361-z. ISSN 0959-3993. PMID 29124367. S2CID 255130139.
- ^ a b Aguilar, C.F.; Cronin, N.B.; Badasso, M.; Dreyer, T.; Newman, M.P.; Cooper, J.B.; Hoover, D.J.; Wood, S.P.; Johnson, M.S.; Blundell, T.L. (April 1997). "The three-dimensional structure at 2.4 Å resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae". Journal of Molecular Biology. 267 (4): 899–915. doi:10.1006/jmbi.1996.0880. ISSN 0022-2836. PMID 9135120.
External links
[edit]- Saccharopepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
