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

Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen.

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
Search PMC articles PubMed articles NCBI proteins

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 (11): 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.

External links

• Rhizopuspepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)