Renal tissue kallikrein
Tissue kallikrein | |||||||||
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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 | ||||||||
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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 Enzymol. 80: 493–532. doi:10.1016/s0076-6879(81)80042-0. PMID 7043199.
- ↑ Anundi, H.; Ronne, H.; Peterson, P.A.; Rask, L. (1982). "Partial amino-acid sequence of the epidermal growth-factor-binding protein". Eur. J. Biochem. 129: 365–371. doi:10.1111/j.1432-1033.1982.tb07059.x. PMID 6295764.
- ↑ Pesquero, J.L.; Boschcov, P.; Oliveira, M.C.F.; Paiva, A.C.M. (1982). "Effect of substrate size on tonin activity". Biochem. Biophys. Res. Commun. 108: 1441–1446. doi:10.1016/s0006-291x(82)80068-5. PMID 6295383.
- ↑ Gutkowska, J.; Corvol, P.; Figueiredo, A.F.S.; Inagami, T.; Bouhnik, J.; Genest, J. (1984). "Kinetic studies of rat renin and tonin on purified rat angiotensinogen". Can. J. Biochem. Cell Biol. 62: 136–142. PMID 6097352.
- ↑ Kato, H.; Enjyoji, K.; Miyata, T.; Hayashi, I.; Oh-Ishi, S.; 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. doi:10.1016/s0006-291x(85)80157-1. PMID 3844939.
- ↑ Akiyama, K.; Nakamura, T.; Iwanaga, S.; Hara, M. (1987). "The chymotrypsin-like activity of human prostate-specific antigen, γ-seminoprotein". FEBS Lett. 225: 168–172. doi:10.1016/0014-5793(87)81151-1. PMID 3691800.
- ↑ Evans, B.A.; Drinkwater, C.C.; 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. doi:10.1111/j.1432-1033.1987.tb10801.x. PMID 3643848.
- ↑ Fujinaga, M.; 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. doi:10.1016/0022-2836(87)90658-9. PMID 2821276.
- ↑ Kato, H.; Nakanishi, E.; Enjyoji, K.; Hayashi, I.; Oh-ishi, S.; 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 3482210.
- ↑ Bailey, G.S. (1989). "Rat pancreas kallikrein". Methods Enzymol. 163: 115–128. doi:10.1016/0076-6879(88)63013-8. PMID 3237072.
- ↑ Blaber, M.; Isackson, P.J.; Marsters, J.C.; Jr.; Burnier, J.P.; Bradshaw, R.A. (1988). "Substrate specificities of growth factor associated kallikreins of the mouse submandibular gland". Biochemistry. 28: 7813–7819. doi:10.1021/bi00445a043. PMID 2611215.
- ↑ Chao, J.; Chao, L. (1988). "Rat urinary kallikrein". Methods Enzymol. 163: 128–143. doi:10.1016/0076-6879(88)63014-x. PMID 3070295.
- ↑ Geiger, R.; Miska, W. (1988). "Human tissue kallikrein". Methods Enzymol. 163: 102–115. doi:10.1016/0076-6879(88)63012-6. PMID 3237071.
- ↑ Bertrand, R.; Derancourt, J.; 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. doi:10.1016/0014-5793(89)80277-7. PMID 2523317.
- ↑ Wines, D.R.; Brady, J.M.; Pritchett, D.B.; Roberts, J.L.; 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.; Gauthier, F. (1990). "Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland". FEBS Lett. 265: 137–140. doi:10.1016/0014-5793(90)80903-v. PMID 2194829.
- ↑ Xiong, W.; Chen, L.-M.; Chao, J. (1990). "Purification and characterization of a kallikrein-like T-kininogenase". J. Biol. Chem. 265: 2822–2827. PMID 2303430.
External links
- Tissue kallikrein at the US National Library of Medicine Medical Subject Headings (MeSH)
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