Carboxypeptidase B2

Carboxypeptidase B2 (CPB2), also known as thrombin-activatable fibrinolysis inhibitor (TAFI), is an enzyme that in humans is encoded by the CPB2 gene. It is a member of the peptidase M14 family of metalloproteases.

Function

Carboxypeptidase B2 is a plasma proenzyme that is activated by thrombin and thrombomodulin and plays a crucial role in the regulation of fibrinolysis and inflammation. It removes C-terminal arginine and lysine residues from biomolecules and proteins. This action can lead to several functional changes in the substrates, such as decreased receptor binding and reduced biological activity.

Clinical significance

Alterations in the CPB2 gene have been associated with thrombophilia due to abnormal fibrinolysis, which can cause thrombosis or hemorrhage. In addition, CPB2 has been implicated in the pathogenesis of sepsis and inflammation.

Structure

The CPB2 gene is located on the long arm of chromosome 13 (13q14.11). The protein encoded by this gene is a zinc carboxypeptidase that catalyzes the removal of basic amino acids from the C-terminus of peptides and proteins. The protein is synthesized as a zymogen that is activated to its functional form by proteolytic cleavage.

See also

• Carboxypeptidase
• Fibrinolysis
• Thrombophilia

External links

• NCBI Gene
• UniProt

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