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.[3]
Kallikrein, a group of enzymes that cleave peptide bonds in proteins
References
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↑Chung DW, Fujikawa K, McMullen BA, Davie EW (August 1986). "Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats". Biochemistry. 25 (9): 2410–7. doi:10.1021/bi00357a017. PMID3521732.
↑Page JD, You JL, Harris RB, Colman RW (October 1994). "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. doi:10.1006/abbi.1994.1424. PMID7944388.
↑Herwald H, Jahnen-Dechent W, Alla SA, Hock J, Bouma BN, Müller-Esterl W (July 1993). "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. PMID7686159.
↑Renné T, Dedio J, Meijers JC, Chung D, Müller-Esterl W (September 1999). "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. doi:10.1074/jbc.274.36.25777. PMID10464316.
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2anw: Expression, crystallization and three-dimensional structure of the catalytic domain of human plasma kallikrein: Implications for structure-based design of protease inhibitors
2any: Expression, Crystallization and the Three-dimensional Structure of the Catalytic Domain of Human Plasma Kallikrein: Implications for Structure-Based Design of Protease Inhibitors