KINE 2011 Lecture Notes - Lecture 16: Cellular Respiration, Cytochrome C Oxidase, Enzyme
24 Oct 2017
School
Department
Course
Professor
Document Summary
Co(cid:373)petitive & (cid:374)o(cid:374)-(cid:272)o(cid:373)petitive i(cid:374)hi(cid:271)itio(cid:374) o(cid:374) e(cid:374)zy(cid:373)e a(cid:272)tivity: competitive inhibitors: presence of inhibitor decreases rate of normal substrate-dependant rnx, molecule competes w/ substrate for enzymes active site- enables products to be formed, inhibitors can be toxic. Cyanide is poison b/c its competes w cytochrome oxidase (enzyme involved cellular respiration: ex: antibiotic drugs act by inhibiting specific bacterial enzymes, non-co(cid:373)petiti(cid:448)e regulatio(cid:374): do(cid:374)"t (cid:272)o(cid:373)pete (cid:449)/su(cid:271)strate for a(cid:272)ti(cid:448)e site. Bind to another location on enzymes: interaction w/enzyme can cause increase or decrease in enzyme. Allosteric inhibitor: converts from high to low affinity state. Allosteric activator: converts from low to high affinity state: allosteric site: location on enzyme outside of active sire, enzymes by non-competitive regulation are called allosteric, allosteric 2 conformations: Metabolism controlled by non-competitive regulations: for metabolism to work efficiently, activity of enzymes must be adjusted- amount of must meet needs of cell, when excess of product produced, its effect as an inhibitor slows/stops enzymes activity.
