Renal tissue kallikrein (EC3.4.21.35, 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).
↑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. PMID6295383.
↑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. PMID6097352.
↑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. PMID3844939.
↑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. PMID2821276.
↑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. PMID3482210.