| Rhodotorulapepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.26 | ||||||||
| CAS no. | 37259-59-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Rhodotorulapepsin ( EC 3.4.23.26, Rhodotorula aspartic proteinase, Cladosporium acid protease, Cladosporium acid proteinase, Cladosporium aspartic proteinase, Paecilomyces proteinase, Rhodotorula glutinis aspartic proteinase, Rhodotorula glutinis acid proteinase, Rhodotorula glutinis aspartic proteinase II, Rhodotorula acid proteinase) is an enzyme. [1] [2] [3] [4] [5] [6] [7] [8] This enzyme catalyses the following chemical reaction
- Specificity similar to that of pepsin A. Cleaves Z-Lys-Ala-Ala-Ala and activates trypsinogen
This enzyme is present in yeast Rhodotorula glutinis.
- ^ Sawada, J. (1963). "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: 677–683. doi: 10.1080/00021369.1963.10858167.
- ^ Sawada, J. (1964). "The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on synthetic substrates". Agric. Biol. Chem. 28: 869–875. doi: 10.1080/00021369.1964.10858312.
- ^ Kamada M, Oda K, Murao S (1972). "The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties". Agric. Biol. Chem. 36 (7): 1095–1101. doi: 10.1271/bbb1961.36.1095.
- ^ Murao S, Funakoshi S, Oda K (1972). "Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2". Agric. Biol. Chem. 36 (8): 1327–1333. doi: 10.1271/bbb1961.36.1327.
- ^ Oda K, Kamada M, Murao S (1972). "Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24". Agric. Biol. Chem. 36 (7): 1103–1108. doi: 10.1271/bbb1961.36.1103.
- ^ Oda K, Funakoshi S, Murao S (1973). "Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2". Agric. Biol. Chem. 37 (7): 1723–1729. doi: 10.1271/bbb1961.37.1723.
- ^ Takahashi K, Chang WJ (September 1976). "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". Journal of Biochemistry. 80 (3): 497–506. doi: 10.1093/oxfordjournals.jbchem.a131304. PMID 10290.
- ^ Majima E, Oda K, Murao S, Ichishima E (1988). "Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate". Agric. Biol. Chem. 52 (3): 787–793. doi: 10.1271/bbb1961.52.787.
- Rhodotorulapepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Rhodotorulapepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.26 | ||||||||
| CAS no. | 37259-59-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Rhodotorulapepsin ( EC 3.4.23.26, Rhodotorula aspartic proteinase, Cladosporium acid protease, Cladosporium acid proteinase, Cladosporium aspartic proteinase, Paecilomyces proteinase, Rhodotorula glutinis aspartic proteinase, Rhodotorula glutinis acid proteinase, Rhodotorula glutinis aspartic proteinase II, Rhodotorula acid proteinase) is an enzyme. [1] [2] [3] [4] [5] [6] [7] [8] This enzyme catalyses the following chemical reaction
- Specificity similar to that of pepsin A. Cleaves Z-Lys-Ala-Ala-Ala and activates trypsinogen
This enzyme is present in yeast Rhodotorula glutinis.
- ^ Sawada, J. (1963). "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: 677–683. doi: 10.1080/00021369.1963.10858167.
- ^ Sawada, J. (1964). "The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on synthetic substrates". Agric. Biol. Chem. 28: 869–875. doi: 10.1080/00021369.1964.10858312.
- ^ Kamada M, Oda K, Murao S (1972). "The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties". Agric. Biol. Chem. 36 (7): 1095–1101. doi: 10.1271/bbb1961.36.1095.
- ^ Murao S, Funakoshi S, Oda K (1972). "Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2". Agric. Biol. Chem. 36 (8): 1327–1333. doi: 10.1271/bbb1961.36.1327.
- ^ Oda K, Kamada M, Murao S (1972). "Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24". Agric. Biol. Chem. 36 (7): 1103–1108. doi: 10.1271/bbb1961.36.1103.
- ^ Oda K, Funakoshi S, Murao S (1973). "Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2". Agric. Biol. Chem. 37 (7): 1723–1729. doi: 10.1271/bbb1961.37.1723.
- ^ Takahashi K, Chang WJ (September 1976). "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". Journal of Biochemistry. 80 (3): 497–506. doi: 10.1093/oxfordjournals.jbchem.a131304. PMID 10290.
- ^ Majima E, Oda K, Murao S, Ichishima E (1988). "Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate". Agric. Biol. Chem. 52 (3): 787–793. doi: 10.1271/bbb1961.52.787.
- Rhodotorulapepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)