Rodotorulapepsin
| Rodotorulapepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.23.26 | ||||||||
| CAS broj | 37259-59-9 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Rodotorulapepsin (EC 3.4.23.26, Rhodotorula aspartinska proteinaza, Cladosporium kiselinska proteaza, Cladosporium kiselinska proteinaza, Paecilomyces proteinaza, Cladosporium aspartinska proteinaza, Paecilomyces proteinaza, Rhodotorula glutinis aspartinska proteinaza, Rhodotorula glutinis kiselinska proteinaza, Rhodotorula glutinis aspartinska proteinaza II, Rhodotorula kiselinska proteinaza) je enzim.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Specifičnost je slična sa pepsinom A. Razlaže se Z-Lys-Ala-Ala-Ala i aktivira se tripsinogen
Ovaj enzim je prisutan u kvascu 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.
- ↑ 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.
- ↑ Kamada, M., Oda, K. and Murao, S. (1972). „The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties”. Agric. Biol. Chem. 36: 1095-1101.
- ↑ Murao, S., Funakoshi, S. and Oda, K. (1972). „Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2”. Agric. Biol. Chem. 36: 1327-1333.
- ↑ Oda, K., Kamada, M. and Murao, S. (1972). „Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24”. Agric. Biol. Chem. 36: 1103-1108.
- ↑ Oda, K., Funakoshi, S. and Murao, S. (1973). „Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2”. Agric. Biol. Chem. 37: 1723-1729.
- ↑ Takahashi, K. and Chang, W.-J. (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”. J. Biochem. (Tokyo) 80: 497-506. PMID 10290.
- ↑ Majima, E., Oda, K., Murao, S. and 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: 787-793.
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.