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Serine Protease

Molecular classification: Enzyme, Protease, Hydrolase

Overview

Serine proteases are a large family of enzymes that cleave peptide bonds in proteins. Their defining feature is the use of a serine residue in their active site, which acts as a nucleophile during catalysis. These enzymes are found across all domains of life and play critical roles in diverse physiological processes such as digestion, blood coagulation, immune response, apoptosis, development regulation, and fertilization. They are regulated by endogenous inhibitors and dysregulation can lead to diseases.

Other names: Serine endopeptidase

Mechanism of action

Nucleophilic attack by activated serine residue, leading to peptide bond hydrolysis.

Biological functions

Protein metabolism/digestionBlood coagulation cascadeImmune system modulationApoptosis inductionRegulation of development/fertilizationActivation of Protease Activated Receptors (PARs)

Disease associations

CoagulopathiesInflammatory disordersCancerOther

Safety considerations

Dysregulation can lead to diseases.Off-target effects due to broad substrate specificity of some serine proteases.Potential for bleeding complications when targeting coagulation factors.

Interacting drugs

Serpins

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