Renal tissue kallikrein

Tissue kallikrein
Identifiers
EC number 3.4.21.35
CAS number 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

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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 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 = Revue Canadienne De Biochimie Et Biologie Cellulaire. 62 (2–3): 137–42. PMID 6097352.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ Bailey GS (1989). "Rat pancreas kallikrein". Methods in Enzymology. 163: 115–28. doi:10.1016/0076-6879(88)63013-8. PMID 3237072.
  12. ↑ 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.
  13. ↑ Chao J, Chao L (1988). "Rat urinary kallikrein". Methods in Enzymology. 163: 128–43. doi:10.1016/0076-6879(88)63014-x. PMID 3070295.
  14. ↑ Geiger R, Miska W (1988). "Human tissue kallikrein". Methods in Enzymology. 163: 102–15. doi:10.1016/0076-6879(88)63012-6. PMID 3237071.
  15. ↑ 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.
  16. ↑ 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.
  17. ↑ 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.
  18. ↑ 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.
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