Question

7. The HIV protease structure was solved very early in the process of developing anti-HIV drugs Importantly, the protease was found to be quite similar to proteases like chymotrypsin and trypsin. Compare and contrast the catalytic mechanism and binding properties of chymotrypsin trypsin, and the HIV protease.

Answer 1

Ams. Catalizie mechanism - el matrypsin: Chymotrypsin is a digestive enzyna duced and released by pancreas. It functions withers Undestime to help break down large protein andecules of Our food. Chymotryprin scute foregor protein metal from where trypten cut. Chymotrypsim makes ele ved at position along the protein chain that contain very large amino acide such as phenylalamenie, tyrosime , tryclophan. Otherwise it is emelar to truppain. (6 rypsin: Trypsin helps to break down large protein medlecules by cutting protein chaine at specific sites. the large protein molecule is actually a chain of Smaller units called amino acide which are linked cond to end in chaine hundreds. There are 20 different amino acids from which there protein chains are made. The specific site along the chain where trysin is active are those with the amèno acide lysine and arrgemeine, two of the smallere amino acids. © HIV preative; HIV prólease breaks down proteins into Smaller protein units. These smaller prolong combine with Hilv's ganolic material to form a New HIV virus. HiN protease involves in peptide bond hydrolysis in retroviṛures. These retroviruses cause ALDS. Hiv prolvase leaves meaceys synthesized polyproteins at nune cleavage sites to create the matura protein campaments of an HIV virón. Binding prosperlies; @ Chymotrypsim: Claymotrypsim cleaves peptide amide bands cchere the sede chain of the amino acid N-terminal to the scissile amede band (the Pi position) is a large hydrophobic amino acido These amino acids contain an aromatee ring in their site chain that fits into a hydrophobu pocket (the si portion of the enzynne, It is activated in the presence of trypsin, The hydrophobic and shape complementary between the peplide substrate Piside chain and enzymes

bindino of thin of this enzyme. wanity accounts for the substrate specificity Trypsim: The negative aspartate residue (Asp 189) located in the catalytic packet (31) of trypsim is responsible for attracting and stabilizing positively charged lysine and/or arginine, and in thes, responsible for the specificity of the enzyme. Truppsin is considered an endopeptidase ie; cleaceage fociures within the polypeptide whain. ② tlv protease: As an aspartie protease, the dimerized HIV protease functions through the aspartyl group complex, in order to perform hydrolyses of the two Aspas residues on the combined catalytic active site of HIV protease, one is deprotonated while the other is protamated . - X