Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
Reaction(IUBMB)
Specificity similar to that of pepsin A. Cleaves Z-Lys!Ala-Ala-Ala and activates trypsinogen
Comment
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].
History
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)
Reference
1
Authors
Sawada, J.
Title
Studies on the acid-protease of Paecilomyces varioti Bainier TPR-220. Part I. Crystallization of the acid-protease of Paecilomyces varioti Bainier TPR-220.
Journal
Agric Biol Chem 27:677-683 (1963)
Reference
2
Authors
Sawada, J.
Title
The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on synthetic substrates.
Journal
Agric Biol Chem 28:869-875 (1964)
Reference
3
Authors
Kamada, M., Oda, K. and Murao, S.
Title
The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties.
Journal
Agric Biol Chem 36:1095-1101 (1972)
Reference
4
Authors
Murao, S., Funakoshi, S. and Oda, K.
Title
Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2.
Journal
Agric Biol Chem 36:1327-1333 (1972)
Reference
5
Authors
Oda, K., Kamada, M. and Murao, S.
Title
Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24.
Journal
Agric Biol Chem 36:1103-1108 (1972)
Reference
6
Authors
Oda, K., Funakoshi, S. and Murao, S.
Title
Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2.
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.
