Conformation of substrates during hydrolysis at the active site of chymotrypsin was written by Lawson, William B.. And the article was included in Journal of Biological Chemistry in 1967.Product Details of 1646-27-1 This article mentions the following:
The quasi axial Me D-hydrocoumarilate compares favorably with Me N-acetyl-L-phenylalaninate as a substrate for chymotrypsin in contrast to the planar Me coumarilate and Me indene-2-carboxylate and the quasi axial Me indan-2-carboxylate, which are either not substrates or very poor substrates. These results lead to the conclusion that Me D-dihydroisocarbostyril-3-carboxylate and Me D-3,4-dihydroisocoumarin-3-carboxylate are in the axial conformation during hydrolysis of chymotrypsin and that typical open-chain substrates, such as Me N-acetyl-L-phenylalaninate, must assume a conformation at the active site somewhat similar to that of these sterically restricted cyclic analogs. It is further proposed that a H bond donor (in addition to the hydrophobic binding site) at the active center of chymotrypsin influences the orientation of substrates and site-specific irreversible inhibitors. 24 references In the experiment, the researchers used many compounds, for example, Methyl benzofuran-2-carboxylate (cas: 1646-27-1Product Details of 1646-27-1).
Methyl benzofuran-2-carboxylate (cas: 1646-27-1) belongs to benzofurans derivatives. Benzofuran derivatives have shown many biological activities, including antifungal and antimicrobial properties, and acting as antagonists of H3 receptors and angiotensin II. Benzofurans are stable towards alkali and readily polymerize on treatment with sulfuric acid, due to which they are useful for the preparation of low cost chemically relatively inert resins.Product Details of 1646-27-1
Referemce:
Benzofuran – Wikipedia,
Benzofuran | C8H6O – PubChem