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Biochemistry Exam 2: Thermodynamics, Enzymes, and Glycolysis, Exams of Biochemistry

This document covers topics related to Biochemistry Exam 2, including the first and second laws of thermodynamics, bioenergetics, thermodynamics, spontaneous processes, free energy change, enzyme function, enzyme catalysis, cofactors, coenzymes, prosthetic groups, ribozymes, enzyme inhibitors, active transport, and glycolysis. It also includes examples and definitions related to each topic. useful for students studying biochemistry and related fields.

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2023/2024

Available from 02/08/2024

Amanda4721
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Download Biochemistry Exam 2: Thermodynamics, Enzymes, and Glycolysis and more Exams Biochemistry in PDF only on Docsity! Exam 2 Biochem (weeks 5 and 6) first law of thermodynamics - ANS The principle of conservation of energy. Energy can be transferred and transformed, but it cannot be created or destroyed. examples to review: cellular respiration and. photosynthesis second law of thermodynamics - ANS Every energy transfer or transformation increases the entropy of the universe. Entropy - ANS a measure of the disorder of a system Bioenergetics - ANS the study of how energy flows through living organisms (energy involved in making and breaking of chemical bonds) Property of all living organisms - ANS the ability to harness energy from a variety of metabolic pathways Thermodynamics - ANS the study of energy transformations isolated system - ANS A system that can exchange neither energy nor matter with its surroundings. ex: liquid in a thermos open system - ANS a system in which exchanges of matter or energy occur between the system and its surroundings Organisms are open systems Spontaneous processes occur - ANS without energy input; they can happen quickly or slowly free energy change (delta G) - ANS a measure of the change in free energy as a chemical reaction or physical change occurs negative delta G - ANS spontaneous, exergonic, favorable, exothermic, entropy increases Most catabolic reactions are - ANS exergonic exergonic reaction - ANS A spontaneous chemical reaction in which there is a net release of free energy. endergonic reaction - ANS A non-spontaneous chemical reaction in which free energy is absorbed from the surroundings. Most anabolic reactions are - ANS endergonic (require ATP) positive delta G - ANS non-spontaneous, endergonic, unfavorable, endothermic, entropy decreases energy coupling - ANS The use of an exergonic process to drive an endergonic one. cell does three main kinds of work - ANS 1. Chemical 2. Transport 3. Mechanical energy coupling in cells is mediated by - ANS ATP ATP in coupled reactions - ANS Energy released by an exergonic reaction (or reactions) is captured in ATP. ATP is then used to drive an endergonic reaction. Enzymes are - ANS proteins that function as catalysts enzyme function - ANS speed up chemical reactions by lowering activation energy delta G at equilibrium - ANS delta G = 0 enzyme catalysis - ANS the increase in the rate of a chemical reaction by the active site of a protein Enzymes - ANS increase reaction rates without being used up Some RNA also catalyze reactions, they are - ANS Ribozymes and Ribosomal RNA The oldest field of biochemistry (dating back to 1700s) is - ANS the study of enzymatic processes In catalyzed reactions - ANS -activation energy decreases -delta G (free energy ) does not change - reaction rate increases -enzymes do not affect equilibrium - enzymes bind best to transition state In catalyzed reactions - ANS -enzyme uses binding energy of substrates to organize reactants to a fairly rigid ES complex -entropy cost is paid during binding -rigid reactant complex --> transition state conversion is entropically neutral proximity model - ANS Enzymes organize reactants into close proximity and proper orientation (work by Thomas C Bruices group) Cofactors - ANS -nonprotein enzyme helpers -usually metal ions connected temporarily or transiently to enzyme -stabilizes negative charges Enzyme active sites are - ANS complimentary to the transition state of the reaction Fischer Mechanism - ANS Active site fixed in shape Kochland's Induced Fit theory - ANS -active site adapts to substrate -active site of induced fit enzymes becomes complementary only after the substrate is bound Coenzymes are - ANS organic molecules connected temporarily or transiently to enzyme -they are often vitamins or derivatives of vitamins prosthetic group - ANS A cofactor or coenzyme that is covalently bonded to a protein to permit its function - connected permanently to enzymes -Examples: FAD or Heme Ribozymes - ANS -catalytic RNA molecules that function as enzymes and can splice RNA -splicing in the tRNA molecules is carried by tRNA itself, and doesn't require a spliceosome -rRNA in the ribosomes carries the peptide bond formation of the ribosomes Rate of enzymatic reaction is affected by: - ANS -temperature -enzyme -substrate concentration -effectors (activators/inhibitors) enzyme inhibitors - ANS -substrate imposters that plug up the active site -compounds that decrease an enzymes activity removes Na+ brings in K+ active transport example - ANS Na/K pump Sodium/potassium pump 3 Na+ out 2 K+ in sodium-potassium pump steps - ANS 1. 3 Na+ ions inside the cell bind to the pump. A phosphate group from ATP also binds to the pump. 2. Pump changes shape transporting 3 Na+ ions across the cell membrane. Na+ ions are released outside the cell. 3. 2 K+ ions, outside the cell bind to the pump. The K+ ions are transported across the cell membrane. 4. The phosphate group is released, and the 2 K+ ions are released into the cell. 4 ways glucose is used by living organisms - ANS 1. energy production 2. Storage 3. production of NADPH and pentoses 4. Structural carbohydrate production energy production by glucose - ANS generates energy via oxidation of glucose- short- term energy needs storage - ANS - can be stored in the polymeric form (starch, glycogen)- used for later energy needs Production of NADPH and pentoses - ANS -generates NADPH for use in relieving oxidative stress and synthesizing fatty acids -generates pentose phosphates for use in DNA/RNA biosynthesis structural carbohydrate production - ANS used for generation of alternate carbohydrates used in cell walls of bacteria, fungi, and plants Many organisms can use glucose to generate:• - ANS all the amino acids• membrane lipids• nucleotides in DNA and RNA• cofactors needed for the metabolism Glycolysis - ANS Primary Energy Source of Cells• Central Metabolic Pathway• All Reactions Occur in Cytoplasm• Two Phases• Produces 2 Pyruvates, 2 ATP, 2 NADH What is phase 1 in glycolysis - ANS energy (ATP) investment phase Name all the steps in phase 1 (substrates/enzyme/prods) - ANS Review Isoforms for hexokinase - ANS hexokinase I, II, III, and IV (glucokinase)) Hexokinase - ANS glucose to glucose-6-phosphate example for induced fit model difference between hexokinase and glucokinase - ANS glucokinase is in the liver. Glucose will encounter glucokinase before it encounters hexokinase. Glucokinase has a HIGH VMAX and a HIGH KM, hexokinase is in all other tissues, deals with lower amounts of glucose, so has a LOWER KM (and LOWER VMAX Kinase - ANS An enzyme that transfers phosphate ions from one molecule to another (responsible for phosphoryl group transfer reactions aldose---ketose - ANS phosphoglucoisomerase ketose --- aldose - ANS triose phosphate isomerase PFK - ANS rate limiting enzyme in glycolysis phosphofructokinase what happens to PFK in the presence of low and high ATP - ANS low ATP- enzyme becomes active high ATP-enzyme becomes inactive The end products of glycolysis are - ANS 2 pyruvate, 2 ATP, 2 NADH Where glycolysis takes place - ANS cytoplasm of the cell, no oxygen required Which steps require ATP? - ANS 1 and 3
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