Aminopeptidaza B
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| Aminopeptidaza B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.11.6 | ||||||||
| CAS broj | 9073-92-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Aminopeptidaza B (EC 3.4.11.6, arilamidaza II, argininska aminopeptidaza, arginilna aminopeptidaza, Cl—aktivirana argininska aminopeptidaza, citosolna aminopeptidaza IV, L-argininska aminopeptidaza) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Odvajanje N-terminalnog Arg i Lys sa oligopeptida ka P1' nije Pro. Takođe deluje na arilamide Arg i Lys ostataka
Ovaj citosolni i za membranu vezani enzim iz tkiva sisara aktiviraju joni hlorida i niska koncentratija tiolnih jedinjenja.
Reference[uredi | uredi kod]
- ↑ Gainer, H., Russell, J.T. and Loh, Y.P. (1984). „An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from β-lipotropin(60-65)”. FEBS Lett. 175: 135-139. PMID 6434344.
- ↑ Belhacène, N., Mari, B., Rossi, B. and Auberger, P. (1993). „Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation”. Eur. J. Immunol. 23: 1948-1955. PMID 8344358.
- ↑ Cadel, S., Pierotti, A.R., Foulon, T., Créminon, C., Barré, N., Segrétain, D. and Cohen, P. (1995). „Aminopeptidase-B in the rat testes: Isolation, functional properties and cellular localization in the seminiferous tubules”. Mol. Cell. Endocrinol. 110: 149-160. PMID 7672445.
- ↑ Fukasawa, K.M., Fukasawa, K., Kanai, M., Fujii, S. and Harada, M. (1996). „Molecular cloning and expression of rat liver aminopeptidase B”. J. Biol. Chem. 271: 30731-30735. PMID 8940051.
- ↑ Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noel, N. and Cohen, P. (1997). „Aminopeptidase B from the rat testis is a bifunctional enzyme structually related to leukotriene-A4 hydrolase”. Proc. Natl. Acad. Sci. USA 94: 2963-2968. PMID 9096329.
- ↑ Orning, L., Gierse, J.K. and Fitzpatrick, F.A. (1994). „The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity”. J. Biol. Chem. 269: 11269-11267. PMID 8157657.
Literatura[uredi | uredi kod]
- 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.