The Enzyme Database

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Accepted name: rhizopuspepsin
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. Does not cleave Gln4-His, but does cleave His10┼Leu and Val12┼Glu in B chain of insulin
Other name(s): Rhizopus aspartic proteinase; neurase; Rhizopus acid protease; Rhizopus acid proteinase
Comments: From the zygomycete fungus Rhizopus chinensis. A similar endopeptidase is found in R. niveus [2]. In peptidase family A1 (pepsin A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-09-3
1.  Tsuru, D., Hattori, A., Tsuji, H., Yamamoto, T. and Fukumoto, J. Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis. Agric. Biol. Chem. 33 (1969) 1419–1426.
2.  Kurono, Y., Chidimatsu, M., Horikoshi, K. and Ikeda, Y. Isolation of a protease from a Rhizopus product. Agric. Biol. Chem. 35 (1971) 1668–1675.
3.  Ohtsuru, M., Tang, J. and Delaney, R. Purification and characterization of rhizopuspesin isozymes from a liquid culture of Rhizopus chinensis. Int. J. Biochem. 14 (1982) 925–932. [PMID: 6751894]
4.  Suguna, K., Padlan, E.A., Smith, C.W., Carlson, W.D. and Davies, D.R. 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 (1987) 7009–7013. [DOI] [PMID: 3313384]
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