Renal tissue kallikrein
Appearance
Tissue kallikrein | |||||||||
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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 | ||||||||
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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] This enzyme catalyses the following chemical reaction
- Preferential cleavage of Arg- bonds in small molecule substrates. It acts highly selectively to release kallidin (lysyl-bradykinin) from kininogen
This enzyme is formed from tissue prokallikrein by activation with trypsin.
See also
References
- ^ Fiedler F, Fink E, Tschesche H, Fritz H (1981). "Porcine glandular kallikreins". Methods in Enzymology. 80 Pt C: 493–532. doi:10.1016/s0076-6879(81)80042-0. 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. 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. 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. 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. PMID 3482210.
- ^ Bailey GS (1989). "Rat pancreas kallikrein". Methods in Enzymology. 163: 115–28. doi:10.1016/0076-6879(88)63013-8. 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". Methods in Enzymology. 163: 128–43. doi:10.1016/0076-6879(88)63014-x. PMID 3070295.
- ^ Geiger R, Miska W (1988). "Human tissue kallikrein". Methods in Enzymology. 163: 102–15. doi:10.1016/0076-6879(88)63012-6. 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. 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. 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. 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. PMID 2303430.
External links
- Tissue+kallikrein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)