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, 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.; 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, 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.
  4. ↑ 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.
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