Biology:Plasma kallikrein

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Plasma kallikrein
Identifiers
EC number3.4.21.34
CAS number410538-33-9
Alt. namesserum kallikrein, kininogenin, kallikrein I, kallikrein II, kininogenase, kallikrein, callicrein, glumorin, padreatin, padutin, kallidinogenase, bradykininogenase, panceatic kallikrein, onokrein P, dilminal D, depot-Padutin, urokallikrein, urinary kallikrein
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Plasma kallikrein (EC 3.4.21.34) is an enzyme[1][2][3][4][5] that catalyses the following chemical reaction:

Selective cleavage of some Arg- and Lys- bonds, including Lys-Arg and Arg-Ser in (human) kininogen to release bradykinin

Plasma kallikrein and its precursor are encoded by the KLKB1 gene.[6][7]

This enzyme is formed from prekallikrein (Fletcher factor) by factor XIIa.

Function

Plasma prekallikrein is a glycoprotein that participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation. It is synthesized in the liver and secreted into the blood as a single polypeptide chain. Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond. Plasma kallikrein therefore is composed of a heavy chain and a light chain held together by a disulfide bond. The heavy chain originates from the amino-terminal end of the zymogen and contains 4 tandem repeats of 90 or 91 amino acids. Each repeat harbors a novel structure called the apple domain. The heavy chain is required for the surface-dependent pro-coagulant activity of plasma kallikrein. The light chain contains the active site or catalytic domain of the enzyme and is homologous to the trypsin family of serine proteases. Plasma prekallikrein deficiency causes a prolonged activated partial thromboplastin time in patients.[8]

Interactions

Kallikrein and prekallikrein have been shown to interact with High-molecular-weight kininogen.[9][10][11][12]


References

  1. "[14] Bovine and human plasma prekallikrein". Bovine and human plasma prekallikrein. Methods in Enzymology. 80 Pt C. 1981. pp. 157–72. doi:10.1016/s0076-6879(81)80016-x. ISBN 9780121819804. 
  2. "Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates". Biochemistry 20 (25): 7196–206. December 1981. doi:10.1021/bi00528a022. PMID 6976185. 
  3. "[8] Prekallikrein". Prekallikrein. Methods in Enzymology. 163. 1988. pp. 85–95. doi:10.1016/0076-6879(88)63010-2. ISBN 9780121820640. 
  4. "The cDNA structure of rat plasma kallikrein". DNA 8 (8): 563–74. October 1989. doi:10.1089/dna.1989.8.563. PMID 2598771. 
  5. "Synthesis of tripeptide chloromethyl ketones and examination of their inhibitory effects on plasmin and plasma kallikrein". Chemical & Pharmaceutical Bulletin 37 (11): 3108–11. November 1989. doi:10.1248/cpb.37.3108. PMID 2534361. 
  6. "Identification of human plasma kallikrein gene polymorphisms and evaluation of their role in end-stage renal disease". Hypertension 31 (4): 906–11. April 1998. doi:10.1161/01.hyp.31.4.906. PMID 9535413. 
  7. "Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats". Biochemistry 25 (9): 2410–7. August 1986. doi:10.1021/bi00357a017. PMID 3521732. 
  8. "Entrez Gene: KLKB1 kallikrein B, plasma (Fletcher factor) 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3818. 
  9. "Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain". Proc. Natl. Acad. Sci. U.S.A. 76 (10): 4862–6. October 1979. doi:10.1073/pnas.76.10.4862. PMID 291905. Bibcode1979PNAS...76.4862T. 
  10. "Localization of the binding site on plasma kallikrein for high-molecular-weight kininogen to both apple 1 and apple 4 domains of the heavy chain". Arch. Biochem. Biophys. 314 (1): 159–64. October 1994. doi:10.1006/abbi.1994.1424. PMID 7944388. 
  11. "Mapping of the high molecular weight kininogen binding site of prekallikrein. Evidence for a discontinuous epitope formed by distinct segments of the prekallikrein heavy chain". J. Biol. Chem. 268 (19): 14527–35. July 1993. doi:10.1016/S0021-9258(19)85270-5. PMID 7686159. 
  12. "Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2". J. Biol. Chem. 274 (36): 25777–84. September 1999. doi:10.1074/jbc.274.36.25777. PMID 10464316. 

Further reading

External links