Serine proteases make use of covalent catalysis as well as electrostatic stability of the transition state to achieve rate enhancement.

Question

Quizplus · Accepted Answer

Serine proteases have a catalytic triad consisting of a serine residue, a histidine residue, and an acidic residue. The serine residue attacks the peptide bond in the substrate, forming a covalent intermediate with the carbonyl carbon of the peptide bond. The histidine residue helps to activate the serine residue by serving as a proton acceptor/donor. The acidic residue helps to stabilize the positively charged transition state through electrostatic interactions. Together, these mechanisms contribute to rate enhancement in serine protease catalysis.

Serine Proteases Make Use of Covalent Catalysis as Well as Electrostatic