BMS1011 Lecture Notes - Lecture 1: Glucokinase, Exergonic Reaction, Dont

• School: Monash University
• Department: Health Sciences - BMS
• Course: BMS1011
• Professor: Dr Nirma Samarawickrema

Document Summary

Straight dotted lines = rate of reaction at the start. Vmax = maximal velocity that an enzyme can go to (units: m/s) Km = substrate concentration at vmax (units: m) A measure of the affinity of the enzyme for its substrate. Higher km = lower affinity (enzyme-substrate binding is weaker) Combine with enzyme covalently and no other enzyme-substrate complex can form. Combine reversibly with enzyme and can regain full activity if inhibitor removed (i) Binding of inhibitor prevents target molecule (substrate) to bind. Inhibitor binds to a site other than active site. Binds to both free enzyme and es complex. Km increases bc. decreased efficiency of enzyme-substrate interaction. Kinetics different from michaelis-menten model sigmoidal kinetics. Substrate binding causes conformation change to facilitate substrate binding. Catalyse same reaction but have different amino acid sequence. Usually within a single cell or tissue type.