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TAMU BICH 410 - Enzymes
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FBICH 410 1st Edition Lecture 18Outline of Last Lecture - LipidsOutline of Current Lecture - Enzymeso Enzymes catalyze thermodynamically favorable rxns- provide cells with ability to have kineticcontrol over thermodynamic potentialo Work via 1. Higher rxn rates 2. Milder rxn conditions 3. Greater rxn specifity 4. Capacity for regulationo Classes Oxidoreductase- oxidation/reduction referred to as reductases or dehydrogenases and involve NAD/NADH Transferase- transfer groups 3. Hydrolase- used in hydrolysis rxns Lysase- generates a double bond and used in elimination reactions- often called synthase if run in reverse Isomerase- structural change within molecule Ligase- joining of substrates= synthetaseso Classified by common names, systematic name, and classification numberso Cofactors- often times metal ionso Coenzymers- organic cofactors CoA NAD- often times vitaminso Cosubstrates- transiently attachedo Prosthetic groups- permanently associatedo Regeneration- coenzymes are chemically changed in rxn therefore regenerated via another enzyme for transiently bound cofactors regeneration via a separate phase of the same enzyme rxn for prosthetic groupso Kinetics= timingo Catalysis= structural changes occurring during rxno Free energy concerns concentration, intrinsic equilibrium Enzymes cant change equilibrium only accelerate rxno Transition state diagram/ rxn coordinate diagram- contains forward and reverse groups state,a transition state, and a free energy activationo Transition state is the rate determining step- rate of rxn is proportional to e^(-deltaG/RT) The greater the delta G the slower the rxn bc less molecules have sufficient energy therefore greater T faster rxn Enzymes lower transition state free energyo Enzymes lower activation barrier by same amount for forward and reverse rxno Eyring eqn- rate of the rxn to the activation energyThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute. deltaG=-RTln[vh/kT] deltaG0’=-RTlnKeqo Transition state diagrams are made via reaction rateo Carbonic anhydrase enzyme for


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TAMU BICH 410 - Enzymes

Type: Lecture Note
Pages: 2
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