IUBMB Enzyme Nomenclature

EC 3.4.21.103

Accepted name: physarolisin

Reaction: Milk clotting activity. Preferential cleavage of Gly8Ser in B chain of insulin most rapidly, followed by Leu11Val, Cys(SO3H)19Gly and Phe24Phe. No action on Ac-Phe-Tyr(I)2.

Other name(s): Dictyostelium discoideum aspartic proteinase; Dictyostelium discoideum aspartic proteinase E; Physarum flavicomum aspartic proteinase; Physarum polycephalum acid proteinase; Physarum aspartic proteinase; physaropepsin

Comments: Belongs In peptidase family S53. From the slime mold Physarum polycephalum. Is not inhibited by pepstatin, but is blocked by methyl 2-diazoacetamidohexanoate. Closely similar enzymes are found in Dictyostelium discoideum and P. flavicomum. Formerly included in EC 3.4.23.6.

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, CAS registry number: 94949-28-7

References:

1. Henney, H.R. and Tavana, G. Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum. Exp. Mycol. 6 (1982) 161-170.

2. Murakami-Murofushi, K., Hiratsuka, A. and Ohta, J. A novel acid protease from haploid amoebae of Physarum polycephalum, and its changes during mating and subsequent differentiation into diploid plasmodia. Cell Struct. Funct. 9 (1984) 311-315.

3. North, M.J. and Whyte, A. Purification and characterization of two acid proteinases from Dictyostelium discoideum. J. Gen. Microbiol. 130 (1984) 123-134.

4. Wlodawer, A., Li, M., Gustchina, A., Oyama, H., Dunn, B.M. and Oda, K. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. Acta Biochim. Pol. 50 (2003) 81-102. [PMID: 12673349]

5. Nishii, W., Ueki, T., Miyashita, R., Kojima, M., Kim, Y.T., Sasaki, N., Murakami-Murofushi, K. and Takahashi, K. Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase. Biochem. Biophys. Res. Commun. 301 (2003) 1023-1029. [PMID: 12589815]

[EC 3.4.21.103 created 1992 as EC 3.4.23.27 (EC 3.4.23.6 created 1992 (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978], part incorporated 1992), transferred 2003 to EC 3.4.21.103]


Return to EC 3.4.21 home page
Return to EC 3.4 home page
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page