Kalikrein renalnog tkiva
Kalikrein renalnog tkiva (EC 3.4.21.35, glandularni kalikrein, pankreasni kalikrein, submandibularni kalikrein, submaksilarni kalikrein, bubrežni kalikrein, urinarni kalikrein, kalikrein, pljuvačni kalikrein, kininogenin, kininogenaza, kalikrein, glumorin, padreatin, padutin, kalidinogenaza, bradikininogenaza, depot-padutin, urokalikrein, dilminal D, onokrein P) je enzim.[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Kalikrein renalnog tkiva | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.21.35 | ||||||||
| CAS broj | 389069-73-2 | ||||||||
| 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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- Preferentno razlaganje Arg- veza u supstratima koji su mali molekuli. Visoko selektivno dejstvo kojim se oslobađa kalidin (lizil-bradikinin) iz kininogena putem hidrolize Met- ili Leu-. Enzim pacova je neobičan po tome što se direktno oslobađa bradikinin iz autolognih kininogena razlaganjem dve Arg- veze.
Ovaj enzim se formira iz tkivnog prokalikreina putem aktivacije tripsinom.
Reference uredi
- ↑ Fiedler, F., Fink, E., Tschesche, H. and Fritz, H. (1981). „Porcine glandular kallikreins”. Methods Enzymol. 80: 493-532. PMID 7043199.
- ↑ Anundi, H., Ronne, H., Peterson, P.A. and Rask, L. (1982). „Partial amino-acid sequence of the epidermal growth-factor-binding protein”. Eur. J. Biochem. 129: 365-371. PMID 6295764.
- ↑ Pesquero, J.L., Boschcov, P., Oliveira, M.C.F. and Paiva, A.C.M. (1982). „Effect of substrate size on tonin activity”. Biochem. Biophys. Res. Commun. 108: 1441-1446. PMID 6295383.
- ↑ Gutkowska, J., Corvol, P., Figueiredo, A.F.S., Inagami, T., Bouhnik, J. and Genest, J. (1984). „Kinetic studies of rat renin and tonin on purified rat angiotensinogen”. Can. J. Biochem. Cell Biol. 62: 136-142. PMID 6043136.
- ↑ Kato, H., Enjyoji, K., Miyata, T., Hayashi, I., Oh-Ishi, S. and Iwanaga, S. (1985). „Demonstration of arginyl-bradykinin moiety in rat HMW kininogen: direct evidence for liberation of bradykinin by rat glandular kallikreins”. Biochem. Biophys. Res. Commun. 127: 289-295. PMID 3844939.
- ↑ Akiyama, K., Nakamura, T., Iwanaga, S. and Hara, M. (1987). „The chymotrypsin-like activity of human prostate-specific antigen, γ-seminoprotein”. FEBS Lett. 225: 168-172. PMID 3691800.
- ↑ Evans, B.A., Drinkwater, C.C. and Richards, R.I. (1987). „Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus”. J. Biol. Chem. 262: 8027-8034. PMID 3036794.
- ↑ 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.
- ↑ Fujinaga, M. and James, M.N.G. (1987). „Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 Å resolution”. J. Mol. Biol. 195: 373-396. PMID 2821276.
- ↑ Kato, H., Nakanishi, E., Enjyoji, K., Hayashi, I., Oh-ishi, S. and Iwanaga, S. (1987). „Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes”. J. Biochem. (Tokyo) 102: 1389-1404. PMID 3844939.
- ↑ Bailey, G.S. (1989). „Rat pancreas kallikrein”. Methods Enzymol. 163: 115-128. PMID 3237072.
- ↑ Blaber, M., Isackson, P.J., Marsters, J.C., Jr., Burnier, J.P. and Bradshaw, R.A. (1988). „Substrate specificities of growth factor associated kallikreins of the mouse submandibular gland”. Biochemistry 28: 7813-7819. PMID 2611215.
- ↑ Chao, J. and Chao, L. (1988). „Rat urinary kallikrein”. Methods Enzymol. 163: 128-143. PMID 3070295.
- ↑ Geiger, R. and Miska, W. (1988). „Human tissue kallikrein”. Methods Enzymol. 163: 102-115. PMID 2975076.
- ↑ Bertrand, R., Derancourt, J. and Kassab, R. (1989). „Selective cleavage at lysine of the 50 kDa-20 kDa connector loop segment of skeletal myosin S-1 by endoproteinase Arg-C”. FEBS Lett. 246: 171-176. PMID 2523317.
- ↑ Wines, D.R., Brady, J.M., Pritchett, D.B., Roberts, J.L. and MacDonald, R.J. (1989). „Organization and expression of the rat kallikrein gene family”. J. Biol. Chem. 264: 7653-7662. PMID 2708383.
- ↑ Elmoujahed, A., Gutman, N., Brillard, M. and Gauthier, F. (1990). „Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland”. FEBS Lett. 265: 137-140. PMID 2194829.
- ↑ Xiong, W., Chen, L.-M. and Chao, J. (1990). „Purification and characterization of a kallikrein-like T-kininogenase”. J. Biol. Chem. 265: 2822-2827. PMID 2303430.
Literatura uredi
- 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.
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- 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.