Rhizopuspepsin

Rhizopuspepsin
Identifiers
EC number 3.4.23.21
CAS number 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

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

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

  1. ↑ Tsuru, D., Hattori, A., Tsuji, H., Yamamoto, T. and 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.
  2. ↑ Kurono, Y., Chidimatsu, M., Horikoshi, K. and Ikeda, Y. (1971). "Isolation of a protease from a Rhizopus product". Agric. Biol. Chem. 35: 1668–1675. doi:10.1271/bbb1961.35.1668.
  3. ↑ Ohtsuru, M., Tang, J. and Delaney, R. (1982). "Purification and characterization of rhizopuspesin isozymes from a liquid culture of Rhizopus chinensis". Int. J. Biochem. 14 (10): 925–932. doi:10.1016/0020-711x(82)90077-5. PMID 6751894.
  4. ↑ Suguna, K., Padlan, E.A., Smith, C.W., Carlson, W.D. and Davies, D.R. (1987). "Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action". Proc. Natl. Acad. Sci. USA 84: 7009–7013. doi:10.1073/pnas.84.20.7009. PMC 299218. PMID 3313384.

External links

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