Triptaza
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| Triptaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| alpha1 Triptaza tetramer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.21.59 | ||||||||
| CAS broj | 97501-93-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Triptaza (EC 3.4.21.59, mastocitna proteaza II, kožna triptaza, plućna triptaza, pljuvačna triptaza, mastocitna neutralna proteinaza, mastocitna triptaza, mastocitna neutralna proteinaza, mastocitna serinska proteinaza II, mastocitna proteinaza II, mastocitna serinska proteinazna triptaza, mastocitna proteaza II pacova, triptaza M) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Preferencijalno razlaganje veza: Arg-, Lys-, ali sa ograničenijom specifičnošću od tripsina
Ovaj enzim se javalja kao tetramerni molekul sa visokim afinitetom za heparin u mastocitnim granulama.
- ↑ Tanaka, T., McRae, B.J., Cho, K., Cook, R., Fraki, J.E., Johnson, D.A. and Powers, J.C. (1983). „Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin with peptide 4-nitroanilide and thioester substrates”. J. Biol. Chem. 258: 13552-13557. PMID 6358206.
- ↑ Kido, H., Fukusen, N. and Katunuma, N. (1985). „Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and functions”. Arch. Biochem. Biophys 239: 436-443. PMID 3890754.
- ↑ Cromlish, J.A., Seidah, N.G., Marcinkiewitz, M., Hamelin, J., Johnson, D.A. and Chrétien, M. (1987). „Human pituitary tryptase: molecular forms, NH2-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates”. J. Biol. Chem. 262: 1363-1373. PMID 3543004.
- ↑ Harvima, I.T., Schechter, N.M., Harvima, R.J. and Fräki, J.E. (1988). „Human skin tryptase: purification, partial characterization and comparison with human lung tryptase”. Biochim. Biophys. Acta 957: 71-80. PMID 3140898.
- ↑ Vanderslice, P., Ballinger, S.M., Tam, E.K., Goldstein, S.M., Craik, C.S. and Caughey, G. (1990). „Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family”. Proc. Natl. Acad. Sci. USA 87: 3811-3815. PMID 2187193.
- 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.