Question

Serpins are naturally occurring proteins that serve as serine protease inhibitors. Serpins bind to the enzyme and are cleaved, but the acyl enzyme intermediate cannot behydrolyzed leading to irreversible inhibition. One of the serpins is a potent inhibitor of the serine protease trypsin and, as expected, contains an arginine at the site of cleavage. Using arrows to show the flow of electrons, draw the mechanism for theinhibition of trypsin by this serpin, labeling all intermediates. Draw the side chains of important enzyme amino acids, and show all hydrogen bonding within the enzyme-substrate complex. Also be sure to include the important arginine on the inhibitor including its side chain.

Answer 1

Step-by-step explanation:

The serpins are components of human plasma and its mutations result in numerous genetic diseases, such as caused by the deficiency of α 1 -antitrypsin. They are proteins of high molecular mass (350-500 amino acids) and have been identified in numerous organisms, from viruses to mammals. The serpins interact with the target enzyme by a similar mechanism on a substrate, although an irreversible interaction where the bond occurs serpin adopts different conformations to interact with the protease target, causing a deformation of the active site of the protease.

The mechanism of inhibition of Trypsin by serpin can be seen in the image below.