Tripsin
| Tripsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.21.4 | ||||||||
| CAS broj | 2594141 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Tripsin (EC 3.4.21.4, alfa-tripsin, beta-tripsin, kokunaza, parenzim, parenzimol, triptar, tripur, pseudotripsin, tripcelim, sperm receptorska hidrolaza) je enzim.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Preferentno odvajanje: Arg-, Lys-
Jednolančani polipeptid goveđeg beta-tripsina se formira iz tripsinogena razlaganjem jedne peptidne veze.
Reference
- ↑ Huber, R. and Bode, W. (1978). „Structural basis of the activation and action of trypsin”. Acc. Chem. Res. 11: 114-122.
- ↑ Walsh, K.A. (1970). „Trypsinogens and trypsins of various species”. Methods Enzymol. 19: 41-63.
- ↑ Read, R.J., Brayer, G.D., Jurásek, L. and James, M.N.G. (1984). „Critical evaluation of comparative model building of Streptomyces griseus trypsin”. Biochemistry 23: 6570-6575. PMID 6442164.
- ↑ Fiedler, F. (1987). „Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin”. Eur. J. Biochem. 163: 303-312. PMID 3643848.
- ↑ Fletcher, T.S., Alhadeff, M., Craik, C.S. and Largman, C. (1987). „Isolation and characterization of a cDNA encoding rat cationic trypsinogen”. Biochemistry 26: 3081-3086. PMID 3112218.
- ↑ Polgár, L. (1987). „Structure and function of serine proteases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 159-200.
- ↑ Tani, T., Kawashima, I., Mita, K. and Takiguchi, Y. (1990). „Nucleotide sequence of the human pancreatic trypsinogen III cDNA”. Nucleic Acids Res. 18: 1631-1631. PMID 2326201.
Literatura
- 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.
- Polgár, L. (1987). „Structure and function of serine proteases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 159-200.
Spoljašnje veze
- MeSH Trypsin
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
