BCH210H1 Lecture Notes - Acetaldehyde Dehydrogenase, Pyruvate Dehydrogenase, Alcohol Dehydrogenase

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Catalytic power 103 - 107 times faster than no enzyme. Speeds approach to equilibrium but does not affect equilibrium. Lowers energy barrier, reach transition state faster: enzyme classes a. oxidoreductase: oxidation-reduction reactions eg. lactate dehydrogenase oxidize l-lactate to pyruvate and reduce coenzyme nad+ to nadh. One substrate is oxidized (lose electron) while the other is reduced (gain electron) Reversible b. transferases: group transfer reactions eg. alanine transaminase, carnitine acyltransferase. Kinases carry out phosphorylation reactions -> irreversible, requires atp c. hydrolases: catalyze hydrolysis, use h2o as substrate eg. pyrophosphatase uses water to break pyrophosphate, hydrolysis of anhydride bond (very high energy linkage), gives 2 phosphates. Protease, lipase, nuclease, esterase d. lyases: create a double bond or addition to a double bond eg. pyruvate decarboxylase removes carboxyl group of pyruvate and gives acetaldehyde and co2. Synthases catalyze addition reactions, breaks double bond. Reversible f. ligases: catalyze joining of two molecules eg. addition of nh4+ with l-glutamate to produce l-glutamine.