Renal tissue kallikrein
| Tissue kallikrein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.35 | ||||||||
| CAS no. | 389069-73-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Renal tissue kallikrein (EC 3.4.21.35, glandular kallikrein, pancreatic kallikrein, submandibular kallikrein, submaxillary kallikrein, kidney kallikrein, urinary kallikrein, kallikrein, salivary kallikrein, kininogenin, kininogenase, callicrein, glumorin, padreatin, padutin, kallidinogenase, bradykininogenase, depot-padutin, urokallikrein, dilminal D, onokrein P) is an enzyme.[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][excessive citations]
Renal tissue kallikrein is formed from kidney tissue prokallikrein by activation with the enzyme trypsin. It catalyses the chemical reaction causing preferential cleavage of Arg- bonds in small molecule substrates, acting to highly selectively release kallidin (lysyl-bradykinin, a bioactive kinin) from kininogen (a kinin protein precursor).
References
[edit]- ^ Fiedler F, Fink E, Tschesche H, Fritz H (1981). "Porcine glandular kallikreins". Proteolytic Enzymes, Part C. Methods in Enzymology. Vol. 80 Pt C. pp. 493–532. doi:10.1016/s0076-6879(81)80042-0. ISBN 978-0-12-181980-4. PMID 7043199.
- ^ Anundi H, Ronne H, Peterson PA, Rask L (December 1982). "Partial amino-acid sequence of the epidermal growth-factor-binding protein". European Journal of Biochemistry. 129 (2): 365–71. doi:10.1111/j.1432-1033.1982.tb07059.x. PMID 6295764.
- ^ Pesquero JL, Boschcov P, Oliveira MC, Paiva AC (October 1982). "Effect of substrate size on tonin activity". Biochemical and Biophysical Research Communications. 108 (4): 1441–6. doi:10.1016/s0006-291x(82)80068-5. PMID 6295383.
- ^ Gutkowska J, Corvol P, Figueiredo AF, Inagami T, Bouhnik J, Genest J (1984). "Kinetic studies of rat renin and tonin on purified rat angiotensinogen". Canadian Journal of Biochemistry and Cell Biology. 62 (2–3): 137–42. doi:10.1139/o84-020. PMID 6097352.
- ^ Kato H, Enjyoji K, Miyata T, Hayashi I, Oh-ishi S, Iwanaga S (February 1985). "Demonstration of arginyl-bradykinin moiety in rat HMW kininogen: direct evidence for liberation of bradykinin by rat glandular kallikreins". Biochemical and Biophysical Research Communications. 127 (1): 289–95. doi:10.1016/s0006-291x(85)80157-1. PMID 3844939.
- ^ Akiyama K, Nakamura T, Iwanaga S, Hara M (December 1987). "The chymotrypsin-like activity of human prostate-specific antigen, gamma-seminoprotein". FEBS Letters. 225 (1–2): 168–72. Bibcode:1987FEBSL.225..168A. doi:10.1016/0014-5793(87)81151-1. PMID 3691800.
- ^ Evans BA, Drinkwater CC, Richards RI (June 1987). "Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus". The Journal of Biological Chemistry. 262 (17): 8027–34. doi:10.1016/S0021-9258(18)47521-7. PMID 3036794.
- ^ Fiedler F (March 1987). "Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin". European Journal of Biochemistry. 163 (2): 303–12. doi:10.1111/j.1432-1033.1987.tb10801.x. PMID 3643848.
- ^ Fujinaga M, James MN (May 1987). "Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution". Journal of Molecular Biology. 195 (2): 373–96. doi:10.1016/0022-2836(87)90658-9. PMID 2821276.
- ^ Kato H, Nakanishi E, Enjyoji K, Hayashi I, Oh-ishi S, Iwanaga S (December 1987). "Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes". Journal of Biochemistry. 102 (6): 1389–404. doi:10.1093/oxfordjournals.jbchem.a122185. PMID 3482210.
- ^ Bailey GS (1989). "Rat pancreas kallikrein". Immunochemical Techniques Part M: Chemotaxis and Inflammation. Methods in Enzymology. Vol. 163. pp. 115–28. doi:10.1016/0076-6879(88)63013-8. ISBN 978-0-12-182064-0. PMID 3237072.
- ^ Blaber M, Isackson PJ, Marsters JC, Burnier JP, Bradshaw RA (September 1989). "Substrate specificities of growth factor associated kallikreins of the mouse submandibular gland". Biochemistry. 28 (19): 7813–9. doi:10.1021/bi00445a043. PMID 2611215.
- ^ Chao J, Chao L (1988). "Rat urinary kallikrein". Immunochemical Techniques Part M: Chemotaxis and Inflammation. Methods in Enzymology. Vol. 163. pp. 128–43. doi:10.1016/0076-6879(88)63014-x. ISBN 978-0-12-182064-0. PMID 3070295.
- ^ Geiger R, Miska W (1988). "[101 Human tissue kallikrein". Immunochemical Techniques Part M: Chemotaxis and Inflammation. Methods in Enzymology. Vol. 163. pp. 102–15. doi:10.1016/0076-6879(88)63012-6. ISBN 978-0-12-182064-0. PMID 3237071.
- ^ Bertrand R, Derancourt J, Kassab R (March 1989). "Selective cleavage at lysine of the 50 kDa-20 kDa connector loop segment of skeletal myosin S-1 by endoproteinase Arg-C". FEBS Letters. 246 (1–2): 171–6. Bibcode:1989FEBSL.246..171B. doi:10.1016/0014-5793(89)80277-7. PMID 2523317.
- ^ Wines DR, Brady JM, Pritchett DB, Roberts JL, MacDonald RJ (May 1989). "Organization and expression of the rat kallikrein gene family". The Journal of Biological Chemistry. 264 (13): 7653–62. doi:10.1016/S0021-9258(18)83284-7. PMID 2708383.
- ^ Elmoujahed A, Gutman N, Brillard M, Gauthier F (June 1990). "Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland". FEBS Letters. 265 (1–2): 137–40. Bibcode:1990FEBSL.265..137E. doi:10.1016/0014-5793(90)80903-v. PMID 2194829.
- ^ Xiong W, Chen LM, Chao J (February 1990). "Purification and characterization of a kallikrein-like T-kininogenase". The Journal of Biological Chemistry. 265 (5): 2822–7. doi:10.1016/S0021-9258(19)39875-8. PMID 2303430.
External links
[edit]- Tissue+kallikrein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
