KLKB1 (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. KLKB1 is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond. This protein therefore is composed of a heavy chain and a light chain held together by a disulphide 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 KLKB1. The light chain contains the active site or catalytic domain of the enzyme and is homologous to the trypsin family of serine proteases. KLKB1 deficiency causes a prolonged activated partial thromboplastin time in patients (1).
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