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What class of enzyme is serine protease?

What class of enzyme is serine protease?

Serine proteinases are the largest class of mammalian proteinases. They are so called because they have a catalytically essential serine residue at their active sites. Serine proteinases are optimally active at neutral pH and play major roles in extracellular proteolysis.

Which of the following is a serine protease?

Answer. Chymotrypsin,Trypsin, Elastase are serine proteases.

What is a protease domain?

The PA (Protease associated) domain is found as an insert domain in diverse proteases, which include the MEROPS peptidase families A22B, M28, and S8A. . The PA domain is also found in a plant vacuolar sorting receptor. O22925. and members of the RZF family, e.g.

What is the serine protease family?

The serine proteases are divided into two families: the trypsins and the subtilisins. The trypsin family is the largest and contains, among others, trypsin and chymotrypsin, elastase, mast cell tryptase, and many of the factors regulating blood coagulation and fibrinolysis.

What is the serine protease mechanism?

Serine proteases catalyze peptide bond hydrolysis in two sequential steps. In the first (acylation) reaction, the nucleophilic serine attacks the substrate scissile bond, forming first a tetrahedral intermediate and then a covalent acyl-enzyme with release of the C-terminal fragment.

Is Thrombin a serine protease?

Thrombin is a Na+-activated, allosteric serine protease that plays opposing functional roles in blood coagulation. Binding of Na+ is the major driving force behind the procoagulant, prothrombotic and signaling functions of the enzyme, but is dispensable for cleavage of the anticoagulant protein C.

Is trypsin glycosylated?

Consistently, most of the trypsin superfamily members are N-glycosylated proteins (Bolt et al., 2007; Jiang et al., 2014; Liao et al., 2007; Miyake et al., 2010; Wu and Suttie, 1999).

What type of protein is thrombin?

protease
Thrombin is a protease and a potent physiological activator of platelet aggregation, a process of key significance to both hemostasis and thrombosis. Thrombin acts on protease-activated receptors. At least four protease-activated receptors are known — PAR1–4 — all members of the G-protein-coupled receptor family.

Is thrombin a serine protease?

What is the difference between a serine protease and an aspartate protease?

Aspartic proteases are a group of protease enzymes that use two highly conserved aspartic acid residues in the active site for catalytic cleavage of their peptide substrates. Unlike serine or cysteine proteases these proteases do not form a covalent intermediate during cleavage.