The Enzyme Database

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Accepted name: mucorpepsin
Reaction: Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1′. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen
Other name(s): Mucor rennin; Mucor aspartic proteinase; Mucor acid proteinase; Mucor acid protease; Mucor miehei aspartic proteinase; Mucor miehei aspartic protease; Mucor pusillus emporase; Fromase 100; Mucor pusillus rennin; Fromase 46TL; Mucor miehei rennin
Comments: Isolated from the zygomycete fungi Mucor pusillus and M. miehei. The two species variants show 83% sequence identity and are immunologically crossreactive. In peptidase family A1 (pepsin A family). Formerly included in EC
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 148465-73-0
1.  Arima, K., Yu, J. and Iwasaki, S. Milk-clotting enzyme from Mucor pusillus var. lindt. Methods Enzymol. 19 (1970) 446–459.
2.  Ottesen, M. and Rickert, W. The acid protease of Mucor miehei. Methods Enzymol. 19 (1970) 459–460.
3.  Sternberg, M. Bond specificity, active site and milk cloting mechanism of the Mucor miehei protease. Biochim. Biophys. Acta 285 (1972) 383–392. [DOI] [PMID: 4573298]
4.  Oka, T., Ishino, K., Tsuzuki, H., Morihara, K. and Arima, K. On the specificity of a rennin-like enzyme from Mucor pusillus. Agric. Biol. Chem. 37 (1973) 1177–1184.
5.  Baudy, M., Foundling, S., Pavlik, M., Blundell, T. and Kostka, V. Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment. FEBS Lett. 235 (1988) 271–274. [DOI] [PMID: 3042459]
[EC created 1992 (EC created 1992 (EC created 1961 as EC, transferred 1972 to EC, modified 1981 [EC, EC, EC, EC, EC, EC and EC all created 1972 and incorporated 1978], part incorporated 1992)]

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