BCH210H1 Lecture Notes - Lecture 20: Dd-Transpeptidase, Enzyme Kinetics, Head Injury
rahulravikumar24 and 39857 others unlocked
49
BCH210H1 Full Course Notes
Verified Note
49 documents
Document Summary
Understanding km, vmax, turnover number: lineweaver-burk plots, competitive inhibition: classical / non-classical, non-competitive inhibition, irreversible inhibition. For andreopoulos" section: chapter 12 (except non-linear. High means weak binding: under true m-m conditions, it is an estimate of the dissociation constant of e from s. Alcohol dehydrogenase creates acetylaldehyde allowing for a good time. Acetylaldehyde dehydrogenase (ad) produces acetate and is excreted. Mito ad responsible for carrying out majority of acetate reaction (low km so don"t need a lot) There are mutations where this is rendered inactive. Even a small amount of alcohol can cause problems as acetylaldehyde conc increases. Cyto ad has high km so needs a lot of acetylaldehyde to get started (lots of substrate) Theoretical maximal velocity and is a constant at saturating conditions. Never achieved and represents an asymptote approached as substrate is increased. To reach this, it would require that all enzyme molecules are tightly bound with substrate.