腺性カリクレイン

関: tissue kallikrein

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2018/04/29 20:56:37」(JST)

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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.

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. 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)

UpToDate Contents

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Japanese Journal

血漿および腺性キニン前駆体である高分子および低分子キニノーゲンのcDNA構造解析と遺伝子の形態学的解析

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International journal of urology 13(3), 238-243, 2006-03-01
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Tissue Expression of Glandular Kallikrein and Its Response to 17 β-estradiol in the Acclimatized Carp(Biochemistry) :

Zoological science 23(6), 507-516, 2006
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「腺性カリクレイン」

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Tissue kallikrein
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EC number	3.4.21.35
CAS number	389069-73-2
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　　[★]

英: glandular kallikrein
関: カリクレイン

「glandular」

　　[★]

腺性の、腺の

関: adeno、gland

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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. 102: 1389–1404. PMID 3482210.

[11] Bailey, G.S. (1989). "Rat pancreas kallikrein". Methods Enzymol. 163: 115–128. doi:10.1016/0076-6879(88)63013-8. PMID 3237072.

[12] 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.

[13] Chao, J.; Chao, L. (1988). "Rat urinary kallikrein". Methods Enzymol. 163: 128–143. doi:10.1016/0076-6879(88)63014-x. PMID 3070295.

[14] Geiger, R.; Miska, W. (1988). "Human tissue kallikrein". Methods Enzymol. 163: 102–115. doi:10.1016/0076-6879(88)63012-6. PMID 3237071.

[15] 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.

[16] 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.

[17] 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.

[18] 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.

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin Streptokinase S1P Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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案内

glandular kallikrein