The Enzyme Database

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EC 3.4.21.35     
Accepted name: tissue kallikrein
Reaction: Preferential cleavage of Arg┼ bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met┼ or Leu┼. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg┼ bonds [5]
Other name(s): 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
Comments: Formed from tissue prokallikrein by activation with trypsin. In peptidase family S1 (trypsin family). A large number of tissue kallikrein-related sequences have been reported for rats [16] and mice [7], though fewer seem to exist in other mammals. The few that have been isolated and tested on substrates include mouse γ-renin (EC 3.4.21.54), submandibular proteinase A [2,15], epidermal growth-factor-binding protein, nerve growth factor γ-subunit, rat tonin [3,4,9], submaxillary proteinases A and B [10], T-kininogenase [18], kallikreins k7 and k8 [17] and human prostate-specific antigen (γ-seminoprotein, [6])
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 389069-73-2
References:
1.  Fiedler, F., Fink, E., Tschesche, H. and Fritz, H. Porcine glandular kallikreins. Methods Enzymol. 80 (1981) 493–532. [PMID: 7043199]
2.  Anundi, H., Ronne, H., Peterson, P.A. and Rask, L. Partial amino-acid sequence of the epidermal growth-factor-binding protein. Eur. J. Biochem. 129 (1982) 365–371. [DOI] [PMID: 6295764]
3.  Pesquero, J.L., Boschcov, P., Oliveira, M.C.F. and Paiva, A.C.M. Effect of substrate size on tonin activity. Biochem. Biophys. Res. Commun. 108 (1982) 1441–1446. [DOI] [PMID: 6295383]
4.  Gutkowska, J., Corvol, P., Figueiredo, A.F., Inagami, T., Bouhnik, J. and Genest, J. Kinetic studies of rat renin and tonin on purified rat angiotensinogen. Can. J. Biochem. Cell Biol. 62 (1984) 137–142. [PMID: 6097352]
5.  Kato, H., Enjyoji, K., Miyata, T., Hayashi, I., Oh-Ishi, S. and Iwanaga, S. Demonstration of arginyl-bradykinin moiety in rat HMW kininogen: direct evidence for liberation of bradykinin by rat glandular kallikreins. Biochem. Biophys. Res. Commun. 127 (1985) 289–295. [DOI] [PMID: 3844939]
6.  Akiyama, K., Nakamura, T., Iwanaga, S. and Hara, M. The chymotrypsin-like activity of human prostate-specific antigen, γ-seminoprotein. FEBS Lett. 225 (1987) 168–172. [DOI] [PMID: 3691800]
7.  Evans, B.A., Drinkwater, C.C. and Richards, R.I. Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus. J. Biol. Chem. 262 (1987) 8027–8034. [PMID: 3036794]
8.  Fiedler, F. Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin. Eur. J. Biochem. 163 (1987) 303–312. [DOI] [PMID: 3643848]
9.  Fujinaga, M. and James, M.N.G. Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 Å resolution. J. Mol. Biol. 195 (1987) 373–396. [DOI] [PMID: 2821276]
10.  Kato, H., Nakanishi, E., Enjyoji, K., Hayashi, I., Oh-ishi, S. and Iwanaga, S. 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 (1987) 1389–1404. [PMID: 3482210]
11.  Bailey, G.S. Rat pancreas kallikrein. Methods Enzymol. 163 (1989) 115–128. [PMID: 3237072]
12.  Blaber, M., Isackson, P.J., Marsters, J.C., Jr., Burnier, J.P. and Bradshaw, R.A. Substrate specificities of growth factor associated kallikreins of the mouse submandibular gland. Biochemistry 28 (1988) 7813–7819. [PMID: 2611215]
13.  Chao, J. and Chao, L. Rat urinary kallikrein. Methods Enzymol. 163 (1988) 128–143. [PMID: 3070295]
14.  Geiger, R. and Miska, W. Human tissue kallikrein. Methods Enzymol. 163 (1988) 102–115. [PMID: 2975076]
15.  Bertrand, R., Derancourt, J. and Kassab, R. 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 (1989) 171–176. [DOI] [PMID: 2523317]
16.  Wines, D.R., Brady, J.M., Pritchett, D.B., Roberts, J.L. and MacDonald, R.J. Organization and expression of the rat kallikrein gene family. J. Biol. Chem. 264 (1989) 7653–7662. [PMID: 2708383]
17.  Elmoujahed, A., Gutman, N., Brillard, M. and Gauthier, F. Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland. FEBS Lett. 265 (1990) 137–140. [DOI] [PMID: 2194829]
18.  Xiong, W., Chen, L.-M. and Chao, J. Purification and characterization of a kallikrein-like T-kininogenase. J. Biol. Chem. 265 (1990) 2822–2827. [PMID: 2303430]
[EC 3.4.21.35 created 1965 as EC 3.4.4.21, transferred 1972 to EC 3.4.21.8, part transferred 1981 to EC 3.4.21.35]
 
 


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