Wikipedia
Rhizopuspepsin
Rhizopuspepsin (EC 3.4.23.21, Rhizopus aspartic proteinase, neurase, Rhizopus acid protease, Rhizopus acid proteinase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
| Rhizopuspepsin | |
|---|---|
| Identifiers | |
| EC no. | 3.4.23.21 |
| CAS no. | 2620497 |
| Databases | |
| IntEnz | IntEnz view |
| BRENDA | BRENDA entry |
| ExPASy | NiceZyme view |
| KEGG | KEGG entry |
| MetaCyc | metabolic pathway |
| PRIAM | profile |
| PDB structures | RCSB PDB PDBe PDBsum |
- Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen.
From the zygomycete fungus Rhizopus chinensis. A similar endopeptidase is found in R. niveus [2]. In peptidase family A1 (pepsin A family).
References edit
- ^ Tsuru D, Hattori A, Tsuji H, Yamamoto T, Fukumoto J (1969). "Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis". Agric. Biol. Chem. 33: 1419–1426. doi:10.1080/00021369.1969.10859482.
- ^ Kurono, Y.; Chidimatsu, M.; Horikoshi, K.; Ikeda, Y. (1971). "Isolation of a protease from a Rhizopus product". Agric. Biol. Chem. 35 (11): 1668–1675. doi:10.1271/bbb1961.35.1668.
- ^ Ohtsuru M, Tang J, Delaney R (1982). "Purification and characterization of rhizopuspepsin isozymes from a liquid culture of Rhizopus chinensis". The International Journal of Biochemistry. 14 (10): 925–32. doi:10.1016/0020-711x(82)90077-5. PMID 6751894.
- ^ Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR (October 1987). "Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action". Proceedings of the National Academy of Sciences of the United States of America. 84 (20): 7009–13. doi:10.1073/pnas.84.20.7009. PMC 299218. PMID 3313384.
External links edit
- Rhizopuspepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)