Biology:Plasma kallikrein
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| Plasma kallikrein | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.21.34 | ||||||||
| CAS number | 410538-33-9 | ||||||||
| Alt. names | serum 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 | |||||||||
| 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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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
- ↑ "[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.
- ↑ "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.
- ↑ "[8] Prekallikrein". Prekallikrein. Methods in Enzymology. 163. 1988. pp. 85–95. doi:10.1016/0076-6879(88)63010-2. ISBN 9780121820640.
- ↑ "The cDNA structure of rat plasma kallikrein". DNA 8 (8): 563–74. October 1989. doi:10.1089/dna.1989.8.563. PMID 2598771.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "Entrez Gene: KLKB1 kallikrein B, plasma (Fletcher factor) 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3818.
- ↑ "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. Bibcode: 1979PNAS...76.4862T.
- ↑ "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.
- ↑ "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.
- ↑ "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
- "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. 1980. doi:10.1073/pnas.76.10.4862. PMID 291905. Bibcode: 1979PNAS...76.4862T.
- "Fletcher factor deficiency: report of a new family". Scandinavian Journal of Haematology 21 (2): 94–8. 1978. doi:10.1111/j.1600-0609.1978.tb02498.x. PMID 694428.
- "Immunovisualisation of Plasma Prekallikrein and H-Kininogen on Human Neutrophils and in Human Hepatocytes". Recent Progress on Kinins. Agents and Actions Supplements. 38. Birkhäuser. 1992. pp. 590–4. doi:10.1007/978-3-0348-7321-5_72. ISBN 978-3-0348-7323-9.
- "Gene structure and chromosomal localization of plasma kallikrein". Biochemistry 30 (6): 1628–35. 1991. doi:10.1021/bi00220a027. PMID 1993180.
- "Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule". Biochemistry 30 (8): 2050–6. 1991. doi:10.1021/bi00222a007. PMID 1998666.
- "Purification and characterization of plasma protein C inhibitor". Thromb. Res. 55 (3): 369–84. 1989. doi:10.1016/0049-3848(89)90069-8. PMID 2551064.
- "Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein". Biochemistry 25 (9): 2417–24. 1986. doi:10.1021/bi00357a018. PMID 3636155.
- "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. 1993. doi:10.1016/S0021-9258(19)85270-5. PMID 7686159.
- "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. 1994. doi:10.1006/abbi.1994.1424. PMID 7944388.
- "Assembly of contact-phase factors on the surface of the human neutrophil membrane". Blood 84 (2): 474–82. 1994. doi:10.1182/blood.V84.2.474.474. PMID 8025275.
- "Activation of the zymogen of hepatocyte growth factor activator by thrombin". J. Biol. Chem. 268 (30): 22927–32. 1993. doi:10.1016/S0021-9258(18)41615-8. PMID 8226803.
- "Extra-hepatic transcription of plasma prekallikrein gene in human and rat tissues". Biochem. Biophys. Res. Commun. 197 (3): 1370–6. 1994. doi:10.1006/bbrc.1993.2628. PMID 8280154.
- "Inhibitory properties of a novel human Kunitz-type protease inhibitor homologous to tissue factor pathway inhibitor". Biochemistry 35 (1): 266–72. 1996. doi:10.1021/bi951501d. PMID 8555184.
- "High and low molecular weight kininogen and plasma prekallikrein/plasma kallikrein in villous capillaries of human term placenta". Placenta 17 (4): 223–30. 1996. doi:10.1016/S0143-4004(96)90042-9. PMID 8761966.
- "The heparin binding domain of insulin-like growth factor binding protein (IGFBP)-3 increases susceptibility of IGFBP-3 to proteolysis". Horm. Metab. Res. 31 (2–3): 216–25. 1999. doi:10.1055/s-2007-978722. PMID 10226805.
- "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. 1999. doi:10.1074/jbc.274.36.25777. PMID 10464316.
- "Expression of plasma prekallikrein mRNA in human nonhepatic tissues and cell lineages suggests special local functions of the enzyme". Biol. Chem. 380 (9): 1097–102. 1999. doi:10.1515/BC.1999.136. PMID 10543447.
- "Plasma kallikrein localisation in human blood vessels". Immunopharmacology 44 (1–2): 75–80. 2000. doi:10.1016/S0162-3109(99)00112-5. PMID 10604527.
External links
- Plasma+kallikrein at the US National Library of Medicine Medical Subject Headings (MeSH)
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