Chapter 1A - BluWiki.docVIP

Chapter 1A May 11, 2006 12:28 PM ? Chapter 1A: Biochemistry Enzymes The Kinetic Role of the Enzyme The Two Laws of Thermodynamics: #1: Energy cannot be created or destroyed (but it can be mutated) #2: The disorder (entropy) of the universe tends to increase Gibbs free energy: ΔG = ΔH - TΔS H = enthalpy, which is heat energy (ΔH = ΔE - PΔV) T = temperature S = entropy Standard free energy change (ΔGo) is ΔG with all reactants and products present at 1 M concentration, and pH = 7 ΔGo = -RTlnKeq (K is the ratio of reactants to products at equilibrium) ΔG = ΔGo + RTlnK (so we can relate ΔG to ΔGo) K is the ratio of reactants to products at the time (not at equilibrium) A catalyst lowers the activation energy (Ea) of a reaction without changing the ΔG It lowers the Ea by stabilizing the transition state It does not get consumed in the reaction See diagram: ? ? ? ? ? ? ? Enzyme Structure and Function Facts about enzymes: Most of them are globular 3-D folded proteins (this allows for the specificity of the active site) The active site is shaped such that the transition state of the reaction is stabilized It is so specific shape-wise that it can even recognize different stereoisomers of a molecule Proteases are enzymes which cleave proteins Their active site usually has a serine because its OH group can act as a nucleophile to attack the carbonyl carbon of an amino acid to break the peptide bond A recognition pocket is a site on the cleaving enzyme close to the active site which binds to specific amino acid residues in the substrate and allows the serine in the active site to cut at the right place Ways to regulate enzyme activity: Covalent modification (i.e. phosphorylation/dephosphorylation) The phosphate is usually added to/removed from serine, threonine, or tyrosine Proteolytic cleavage The enzyme is called a zymogen before being activated to form an active enzyme (think GI tract) Association with other polypeptides Sometimes there can be regulatory subunits which bind