Biology 1202B Lecture 7: Biology 1202B Lecture : Biology 1202B Lecture : Biology 1202B Lecture : Biology 1202B Lecture : Biology 1202B Lecture : : Biology 1202B Lecture Mon, Jan. 28/19 – Lecture 7: Catalytic Cycle of Enzymes

• School: Western University
• Department: Biology
• Course: Biology 1202B
• Professor: Niki Sharan

Document Summary

Mon, jan. 28/19 lecture 7: catalytic cycle of enzymes. Cycle 3 lecture 7: catalytic cycle of enzymes. Enzymes have allosteric sites, where activators and inhibitors can bind. If an activator binds to the allosteric site, then the enzymes changes conformation and becomes formidable for the substrate to bind, by increasing the it"s affinity. If an inhibitor binds to the allosteric site, the enzyme changes conformation again, but this time the substrate is unable to bind to the enzyme, and decreases its affinity. Study the interactions of the enzyme and the substrate. Irreversibly bind to the h+/k+ atpase enzyme (non- competitive) and prevent the increase in h+ ions being released to form hcl. This reduces the amount of pepsinogen that is converted to the active enzyme pepsin. Pepsin is responsible for digesting proteins in acid reflux, and reducing the concentration of pepsin ultimately reduces the acid reflux.