BIOC 3560 Study Guide - Final Guide: Glucokinase, Enzyme Inhibitor, Protein Phosphatase

• School: University of Guelph
• Department: Biochemistry
• Course: BIOC 3560
• Professor: Marc Coppolino

Document Summary

Allosteric protein: a protein in which the binding of a ligand to one site affects the binding properties at another site. Allosteric enzyme: a regulatory enzyme with catalytic activity modulated by non-covalent binding of a specific metabolite at a site other than the active site. O2 is a ligand and an activating homotropic modulator: first oxygen binding induces conformational changes, pushing adjacent subunits into the r state, causing higher affinity for o2. Co2 causes negative heterotropic allostery: binds at amino-terminus of hb, forms carbaminohemoglobin, releasing oxygen effectively in the tissues, part of the bohr effect (with h+, releases a hydrogen atom when bound to amino-terminus. Aspartate transcarbamoylase (atcase) c arbamoyl phosphate +aspartate atcase. Atp disrupts ion pair between asp 236 on the c chain and lys 143 on the r chain (these connect the c and r subunits, stabilizing the t state), inducing the r state when bound and activating atcase.