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3 Enzyme and metabolism Enzyme y Molecules that increase the rate of chemical reactions without undergoing any chance themselves. y Enzyme are classified as proteins- body contains 3000 enzymes y Enzymes are catalysts ( they speed up reactions), their primary, secondary and territory structure are essential to their catalyst activity y The catalyst activity can be destroyed under certain conditions that denature the protein they include.  High temp  Low or high ph y Some enzymes are purely proteins, others have two parts that work together- halo enzyme.  Apoenzyme: protein portion of the haloenzyme, the apoenzyme co factors and /or co-enzyme make then the functional haloenzyme.  The non protein part is called a co-factor and can be metals, it is non organic  If the co-factor is organic it is called a co-enzyme. Eg vitamins (slides) y The substance an enzyme works on is called the substrate. A combination of enzyme bound to substrate is the enzymesubstrate complex. y Zymogen: enzymes produced in an inactive form to ensure they exert their effect in the correct area of the body. Eg pepsinogen -> pepsin in stomach.  sometimes inactivated as soon as they have performed their function y Isozymes : different tissue may contain the same enzymes through in a slightly different form. y Enzymes are grouped into 6 main categories according to the type of chemical reaction they catalyse.  Oxidases: catalyse oxidations or oxidation reduction reactions  Transferases: catalyse the transfer from one group to another.  Hydrolase(peptidase): catalyse the hydrolysis of lipids and peptides respectively.  Lyase: Make or break double bonds.  Isomerases: catalyse isomerisation (switching between isomers to glucose, then to fructose.

 Ligase: join molecules together or coupling reaction to more favourable reactions. The enzyme active site: the substrate will bind to a specific part of the enzyme in which it perfectly fits called the active site. It is a small cleft or indentation on protein surface, only enzyme molecules with a specific structure will be able to fit at the binding site. Mechanisms of enzyme activity  Enzyme: contains active site  Substrate: substance, acted upon the enzyme  Product: substance produced by the activity

- Enzyme Action y Reactants bind to the active site in a specific orientation, forming an enzyme substrate complex. y Transition State Facilitation: Interaction between enzyme and substrate forming the product. y Termination: Enzyme is unchanged after the reaction and the product is released. - Transition State: molecules reach a high-energy state, before it can form the lower energy product. - Enzymes reduce the amount of energy we put in. they put stress on the bonds and mimic them to make them feel like a chemical reaction is occurring, this reduces the amount of energy for a reaction to occur. - Factors affecting enzyme activity y Concentration of enzyme: increases lineally, increases reaction rate. y Concentration of Substrate: increasing activity until a maximum. y Temp: decreases either side of optimum temp range. y Ph: Ph range. - Substrate concentration, temp and Ph are constant, though as enzyme concentration doubles so does the reaction rate, it is directly proportional.

- Enzyme concentration, Ph and temp are constant, as substrate concentration increases; reaction rate will also increase until a maximum or saturation point is reached. - If enzyme substrate and Ph are kept constant, and the temp changes reaction rate decreases each side of the optimum temp.

-Different enzymes work at different Ph s, therefore the reaction rate decreases each side of the optimum Ph, (Graph looks like a Ph). - Enzyme Regulation y Gene Coding: the formation of enzymes can be induced or repressed by regulating expression of genes that code for the enzyme. E.g. Coli bacteria in the presence of lactose include = beta-galactosidase. y Irreversible Inhibition: metals carry charge; they can bind to the charge of proteins, and change the structure of the proteins. (Enzymes). y Zymogen Activation: Produce enzyme in an inactive form, secrete them in a certain part of the body and an environmental factor such as the change in Ph, can activate the enzyme. y Chemical Modulation: Enzymes can be activated or inhibited depending on the need of the body. - Control of Enzyme Activity y Competitive Inhibition: binds to the active site not allowing the substrate get in. y Non-Competitive Inhibition: A compound (inhibitor) binds somewhere else on the enzyme, which changes the tertiary structure of the enzyme that prevents substrate binding. y Allosteric Regulation: binding somewhere else on the active site. - Allosteric Activation: Activation or deactivation of the active site by an event that occurs away from the active site, when the substrate binds to the enzyme it can the shape dramatically allowing more active sites quicker. - Feedback Inhibition: Where the competitive inhibitor or allosteric regulator is a product of a reaction, or a product later in the series, which switches off the enzyme, allowing the storage of energy. Enzymes in Medical Diagnosis: when cells diseased or injured, enzymes that are not normally found in the cells can spill out into the blood stream, detecting and measuring the levels of these enzymes can allow us to identify the disease or when it occurred. e.g. Micardial Infarction=MI-Heart Attack - Biosphere: an organism acquires energy and carbon skeleton by one or two methods. y Autotrophic Nutrition (Self Feeder): sustained by the organism itself, does not eat; derive energy and carbon from CO2, light and other nutrients of the body. E.g. plants, photoautotrophs y Heterotrophic Nutrition (other feeder): obtains nutrients from other organisms, almost all dependent on photoautotrophs for food and oxygen, animal eat plants and other animals, fungi/ decomposers.

- Photosynthesis: synthesize organic molecules by using light energy to form CHO and oxygen from carbon dioxide and water. y Predominantly conducted by plants, it occurs in the chloroplast, which contains chlorophyll, which has the capacity to absorb light energy. y 160 billion tonnes of CHO is synthesized each year by photosynthesis. Photosynthesis Light Reaction - Plants take up water, and comes into a section called the thylakoid, chlorophyll is contains in the thylakoid membrane this is where the light energy is absorbed, the water is split where the O2 goes into the atmosphere, and the is now electrons and protons. The light absorbed by the chlorophyll transfers electrons and H+ to NADP+ it also forms ATP (photophosphorylation) which is the energy for the plant. Photosynthesis- Dark: (Calvin Cycle) It occurs in the stoma of the plant, it doesn t use light, though wont work unless the light reaction has worked. The energy of the NADPH and the ATP is used for the dark reaction. Steps in the cycle include: 1. Carbon Fixation: incorporation of three CO2 into organic molecules present in chloroplast. 2. The electrons from NADPH then added to fixed carbons these results in CHO formation. This also requires the addition and energy from the ATP. 3. Three CHO formed together to form glyceraldehyde -3- phosphate. 4. Join two of these together and lose the phosphate and glucose deforms it is then used to from starch etc. Metabolism - The sum total of all the chemical reactions involved in maintaining the dynamic state of the cell. -Catabolism: The breaking down of molecules to supply energy. - Anabolism: The building of new molecules storing them requires energy. Metabolism=Catabolism + Anabolism Catabolism - Cellular Respiration: Consumes oxygen as an reactant to complete the breakdown of variety of organic molecules. - Fermentation: less efficient pathway, leads to partial breakdown of sugars without oxygen. Anabolism - Gluconeogenesis (making new glucose) - Glycogenesis (making glycogen) ATP - Link between anabolic and catabolic process - = Energy

- Energy from the breakdown of macromolecules is captured and stored in the bonds as ATP. It is immediately useable for all body tissues. - The bonds between phosphate groups can be broken through hydrolysis; the reaction releases energy and drives mechanical and chemical reactions. It is now known as adenosine diphosphate. Oxidation Reduction Reactions - Oxidation: Gain of oxygen loss of hydrogen/ loss of electrons - Reduction: Loss of oxygen gain of hydrogen/ gain of electrons. - Redox Reactions: Coupling of oxidation and reduction reactions.

Cellular Respiration - Catabolic pathway, which results in ATP, after the step wise oxidation of substrate molecules. Break down chemical bonds formed through photosynthesis. Needs oxygen. Use of coenzymes to transfer electron from the oxidation of substrates. All the carbon that enters the body leaves as CO2. C6H12->6CO2+6H2O+Energy (ATP+Heat) - It occurs in four metabolic pathways y Glycolysis y Processing pyruvate to acetyl-coA. y Citric Acid Cycle (Krebs Cycle) y Electron transport chain and oxidative phosphorylation. - Glycolysis (Glucose Metabolism) 1. It takes places in the cytosol of the cell 2. The breakdown of glucose (glycolysis) 6 Carbon -> Glucose 3. Into 2 three pyruvate molecules (three carbon) 4. 2 ATP is required for this to occur 5. Through this reaction four ATP are produced and 2 NADH which is an electron carrier 6. Overall net energy field ->2ATP + 2 NADH - Process pyruvate to acetyl-coA. 1. The pyruvate moves into the mitochondria 2. 2 molecules of pyruvate produced from the breakdown of one molecule of glucose are converted into 2 molecules of acetyl-coA (2 carbons per molecule) 3. Per pyruvate molecule 1 CO2 is released and one NADH 4. Overall 2 CO2 and 2 NADH - Citric Acid Cycle 1. Occurs still in the mitochondria matrix 2. Universal carbon molecule acetyl-coA enters the citric acid cycle, it links with oxaloacetate, for each glucose it goes around the cycle twice.

3. Each acetyl comes in and 2 carbons are released so for both, 4 CO2 are released. 4. 3 NADH are formed, 1 FADH and 1 GDP which is equivalent to ATP, for each acetyl-coA. - Summary so far y 4 ATP y 10 NADH y 2 FADH y 6 CO2 molecules. - Electron Transport Chain 1. Heaps of proteins stuck in the membrane are hydrogen impermeable, proteins are known as complex protein, they are electron shuttles. 2. 2 NADH move along the chain and get given to oxygen, which reacts and turns into water. 3. The electrons that moved across the complex protein allow it to get charged, allowing hydrogen to get pumped across the matrix and pulled across the membrane. 4. This causes a gradient increasing in the inner membrane space; the increasing concentration allows energy to be produced. 5. NADH produces 3 ATP and FADH2 produces 2 ATP. 6. Chemiosmotic Theory: As electrons move through the complexes H+ is pumped across the membrane at complexes I, III and IV this establishes a Ph. gradient. Hydrogen moves back down the membrane caused by ATP synthase. Just like water well this produces ATP, every NADH produces 3 ATP- 34 in total. Control of Cellular Respiration - A lack of CO2, accumulation of ATP, which means there is no need for a breakdown of glucose for energy or there is a reduction in the amount of NADH. - May result in a catabolic pathway that does not use oxygen. - Aerobic: with oxygen - Anaerobic: without oxygen. Fermentation - Under anaerobic conditions, various fermentation pathways generate ATP by glycolysis and regulate NAD+ by transferring electrons from NADH to pyruvate or derivatives of pyruvate. y Lactic Acid Fermentation: Pyruvate -> Lactate occurs in human muscle tissue. y Alcohol Fermentation: pyruvate is converted to ethanol in 2 steps. NAD+ is recycled. Aerobic Respiration vs. Fermentation - Both pathways rely on glycolysis to breakdown glucose to initially. - Different energy is produced y Aerobic Respiration-34 ATP

y Fermentation- 2 ATP - Fermentation is faster. More glucose require for fermentation to produce the same amount of energy as respiration. - Organisms may use cellular respiration or both. y Obligate: do what ordered  Anaerobes: cannot survive in O2- bacteria  Aerobes: only carry out aerobic respiration- some bacteria. y Facultative Anaerobes: the ability to switch between fermentation and aerobic respiration- muscle cells. Protein Catabolism When breaking down a protein, the nitrogen is stripped from the amino acid, what is left is known as the carbon skeleton and is taken through the same process as glucose.

Lipid Catabolism Triglycerides are broken into glycerol and fatty acids. y Glycerol enters glycolysis to be broken down. y Fatty acids are catabolized via a process known as B-oxidation. y Huge amount of ATP is produced from fatty acids. Anabolic Pathway Essential amino acids can only be found in what we eat, fatty acids can be made from protein and carbs. Gluconeogenesis Making new glucose primarily occurs in the cytoplasm of the liver. Synthesis of Glycogen Links glucose monomers together to form the branched molecule glycogen made in liver stored in liver and muscles.