ExplorEnz: EC 3.4.23.26

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3.4.23.26

Accepted name:

rhodotorulapepsin

Reaction:

Specificity similar to that of pepsin A. Cleaves Z-Lys┼Ala-Ala-Ala and activates trypsinogen

Other name(s):

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. Somewhat similar enzymes have been isolated from the imperfect yeast-like organism Cladosporium sp. [4,6] and the imperfect fungus Paecilomyces varioti [1,2].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, 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) 787–793.

[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)]