IUBMB Enzyme Nomenclature

EC 3.4.23.26

Accepted name: rhodotorulapepsin

Reaction: Specificity similar to that of pepsin A. Cleaves Z-LysAla-Ala-Ala and activates trypsinogen

Other names: Rhodotorula aspartic proteinase; Cladosporium acid protease; Cladosporium acid proteinase; Paecilomyces proteinase; Cladosporium aspartic proteinase; Paecilomyces proteinase; Rhodotorula glutinis aspartic proteinase; Rhodotorula glutinis acid proteinase; Rhodotorula glutinis aspartic proteinase II; Rhodotorula acid proteinase

Comments: From the imperfect yeast Rhodotorula glutinis. Formerly included in EC 3.4.23.6. Somewhat similar enzymes have been isolated from the imperfect yeast-like organism Cladosporium sp. [4,6] and the imperfect fungus Paecilomyces varioti ([1,2], formerly EC 3.4.99.15)

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, CAS registry number: 37259-59-9

References:

1. Sawada, J. Studies on the acid-protease of Paecilomyces varioti Bainier TPR-220. Part I. Crystallization of the acid-protease of Paecilomyces varioti Bainier TPR-220. Agric. Biol. Chem. 27 (1963) 677-683

2. Sawada, J. The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on synthetic substrates. Agric. Biol. Chem. 28 (1964) 869-875

3. Kamada, M., Oda, K. and Murao, S. The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties. Agric. Biol. Chem. 36 (1972) 1095-1101

4. Murao, S., Funakoshi, S. and Oda, K. Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2. Agric. Biol. Chem. 36 (1972) 1327-1333

5. Oda, K., Kamada, M. and Murao, S. Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24. Agric. Biol. Chem. 36 (1972) 1103-1108

6. Oda, K., Funakoshi, S. and Murao, S. Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2. Agric. Biol. Chem. 37 (1973) 1723-1729

7. Takahashi, K. and Chang, W.-J. The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy)propane and pepstatin. J. Biochem. (Tokyo) 80 (1976) 497-506. [PMID: 10290]

8. Majima, E., Oda, K., Murao, S. and Ichishima, E. Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate. Agric. Biol. Chem. 52 (1988) 787-794

[EC 3.4.23.26 created 1992 (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)]


Return to EC 3.4.23 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