BCH210H1 Lecture Notes - Lecture 18: Nicotinamide Adenine Dinucleotide, Carnitine O-Palmitoyltransferase, Redox
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BCH210H1 Full Course Notes
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For andreopoulos" section: chapter 12 (except non-linear. Q 1, 2, 4, 12ab: ch 13. 5 and 13. 6, ch 14. 1 (p. 479-481); ch. Catalytic power and specificity: the active site: lysozyme. Lecture notes: introduction to enzymes and the active site. Catalyze thermodynamically favourable reactions, causing them to proceed at extraordinary rates. 101 to 1016 change in rate: living systems use enzymes to accelerate and control the rates of vitally important biochemical reactions, enzymes are the agents of metabolic function. Typically enzymes end in -ase: sumner crystallized urease in 1926, almost all enzymes are proteins --> such as ribosome made from rna, classification, nomenclature, kinetics, regulation of e activity coenzymes. Enzyme classifications (6 of them: international union of biochemistry created these classifications, oxidoreductase class: redox reactions (like lactate dehydrogenase) Always uses a coenzyme, usually nad+ --> nicotinamide adenine dinucleotide. One substrate is oxidized, one is reduced: oxidation = loss of elections, reduction = gain of electrons, transferase class: group transfer reactions (like alanine transaminase)
