Kalikrein renalnog tkiva
Izgled
Kalikrein renalnog tkiva | |||||||||
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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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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
- 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.
- ↑ 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.
- 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.