From Surf Wiki (app.surf) — the open knowledge base

Renal tissue kallikrein

Field	Value
Name	Tissue kallikrein
EC_number	3.4.21.35
CAS_number	389069-73-2

Renal tissue kallikrein (, 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.

Renal tissue kallikrein is formed from kidney tissue prokallikrein by activation with the enzyme trypsin. It catalyses the chemical reaction causing preferential cleavage of Arg- bonds in small molecule substrates, acting to highly selectively release kallidin (lysyl-bradykinin, a bioactive kinin) from kininogen (a kinin protein precursor).

References

(1981). "Proteolytic Enzymes, Part C".
(December 1982). "Partial amino-acid sequence of the epidermal growth-factor-binding protein". European Journal of Biochemistry.
(October 1982). "Effect of substrate size on tonin activity". Biochemical and Biophysical Research Communications.
(1984). "Kinetic studies of rat renin and tonin on purified rat angiotensinogen". Canadian Journal of Biochemistry and Cell Biology.
(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.
(December 1987). "The chymotrypsin-like activity of human prostate-specific antigen, gamma-seminoprotein". FEBS Letters.
(June 1987). "Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus". The Journal of Biological Chemistry.
(March 1987). "Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin". European Journal of Biochemistry.
(May 1987). "Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution". Journal of Molecular Biology.
(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.
(1989). "Immunochemical Techniques Part M: Chemotaxis and Inflammation".
(September 1989). "Substrate specificities of growth factor associated kallikreins of the mouse submandibular gland". Biochemistry.
(1988). "Immunochemical Techniques Part M: Chemotaxis and Inflammation".
(1988). "Immunochemical Techniques Part M: Chemotaxis and Inflammation".
(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.
(May 1989). "Organization and expression of the rat kallikrein gene family". The Journal of Biological Chemistry.
(June 1990). "Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland". FEBS Letters.
(February 1990). "Purification and characterization of a kallikrein-like T-kininogenase". The Journal of Biological Chemistry.

Info: Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

ec-3.4.21

Want to explore this topic further?

Ask Mako anything about Renal tissue kallikrein — get instant answers, deeper analysis, and related topics.

Research with Mako

Free with your Surf account

Content sourced from Wikipedia, available under CC BY-SA 4.0.

This content may have been generated or modified by AI. CloudSurf Software LLC is not responsible for the accuracy, completeness, or reliability of AI-generated content. Always verify important information from primary sources.

Report