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74 Cards in this Set
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Catabolism/catabolic reaction |
Larger molecules degraded/broken down into smaller molecules-- releases energy |
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Anabolism/anabolic reaction |
Larger molecules built from smaller molecules- results in formation of cell structures- requires energycara |
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Catalysts |
Chemicals that increase rate of a chemical reaction without becoming part of the products or being consumed in the reaction (enzymes) inhibited by low temps |
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Energy of activation |
Least amount of energy required for a molecule to undergo a chemical reaction |
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How can overcoming resistance to a chemical reaction be achieved? |
Adding a catalyst |
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Substrates |
Reactant molecules-- what fits in the active site of enzymes |
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Enzyme-substrate bond |
Enzyme has a pocket that only fits a particular substrate- enzyme binds to substrate and changes it |
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Enzyme speed |
Number of substrate molecules converted per enzyme per second |
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Simple enzyme |
Consists of protein alone |
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Conjugated enzyme |
Consists of protein and non-protein molecules |
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Apoenzymes |
Inactive enzyme- activation occurs upon binding of an organic or inorganic cofactor--exhibits levels of molecular complexity called primary, secondary, tertiary, or quaternary (same as all enzymes)-- single polypeptide chain undergoes automatic folding process which causes surface to have 3D features |
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Holoenzyme |
Apoenzyme together with its cofactor-- reactivated |
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Active site/ catalytic site |
Pocket where substrate binds with enzyme |
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Induced fit |
Enzyme helps substrate move into the active site through slight changes in shape-- bonds are weak and reversible |
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Metallic cofactors |
Iron, copper, magnesium, manganese, zinc, cobalt, selenium |
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Cofactor |
Non-protein chemical compound or metallic ion required for a protein's biological activity to happen |
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What roles to metals have in enzyme-substrate bonds? |
Activate enzymes, help bring active site and substrate together, and participate in chemical reactions with the enzyme |
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Coenzymes |
Organic cofactors that work in conjunction with apoenzyme to perform alteration of a substrate-- remove chemical group from one substrate and add to another |
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What is the most common component of coenzymes? |
Vitamins |
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How are enzymes classified? |
According to the site of action, type of action and substrate |
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Exoenzymes |
Transported extracellularly where they break down large food molecules or harmful chemicals after synthesis in the cell (cellulose, amylase,penicillinase) |
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Endoenzymes |
Retained and function intracellularly |
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Constitutive enzymes |
Always present and in constant amounts, regardless of the amount of substrate |
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Regulated enzymes |
Production is either induced or repressed based on the amount of substrates or product in the cell |
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Condensation (dehydration) synthesis |
Release one water molecule for each bond made |
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Hydrolysis reaction |
Breaking bonds by adding water |
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Labile |
When enzymes become chemically unstable because of changes in normal conditions |
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What are normal conditions for enzymes? |
Natural temperature, pH, and osmotic pressure |
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Denaturization |
Process by which bonds that maintain native shape of apoenzyme are disrupted-- prevents substrate from attatching |
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Metabolic pathways |
Proceed in systematic, highly regulated manner that maximizes use of available nutrients and energy-- linked series of individual chemical reactions that produce metabolites and lead to final product (linear, cyclic, branched) |
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Competitive inhibition |
Cell supplies a molecule that is the same shape as a normal substrate and can occupy the enzyme's active site, inhibiting the production of products-- enzyme shuts down |
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Allosteric inhibition |
Enzyme has 2 sites: active site and regulatory/allosteric site-- product of another enzyme fits in the regulatory site and causes action site to close, inhibiting substrates from fitting in |
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Non-competitive inhibition |
Does not involve molecule competing for space in active site-- inhibitor bonds to substrate-enzyme complex and prevents it from completing action on substrate |
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Enzyme repression |
Stops synthesis of enzymes when the level of products has built to excess |
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Redox reactions |
Occur in pairs with electron donor and electron acceptor |
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What is hydrogen's role in oxidation reduction? |
Hydrogen atoms donate the electrons(hydrogen atom is a single proton and single electron)-- hydrogen gives up its electron to positively charged molecules, leaving H+ |
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Phosphorylation |
Energy released through transport of electrons is captured through this process which adds inorganic phosphate to ADP converting it to ATP |
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Exergonic reaction |
Releases energy as it goes forward (catabolic)-- electrons are pulled out of atoms and release energy, then electrons are picked up by carriers and transferred through a series of reactions until they reach the final electron acceptor (production of ATP) |
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Endergonic reactions |
Driven forward with the addition of energy(anabolic)-- supported by ATP |
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Oxidation reduction |
Transport of electrons--oxidation=loss of electrons and reduction=gains electrons |
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Enzyme induction |
Enzymes appear only when suitable substrates are present-- prevents the microbe from making an enzyme in which substrates for it are lacking |
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NAD+, FAD, coenzyme A, compounds of respiratory chain |
Accepts electrons from one substrate and donates them to another substrate |
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NAD+ |
Takes 2 electrons and a hydrogen atom to form NADH (reduced NAD+) |
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NADH |
Carrier molecule-- every transfer of electrons from NADH to another carrier molecule makes NAD+ available for redox cycle again |
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ATP |
Adenine triphosphate (adenine linked to ribose with a chain of 3 phosphate groups bonded to ribose) |
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ATP to ADP |
The 3 phosphate groups don't like being together-- one breaks off and makes ADP (adenine diphosphate) |
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AMP |
Component of coenzymes (NAD+,FAD, coenzyme A)-- converted from ADP-- only has one phosphate group |
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Oxidative phosphorylation |
ATP in aerobic organisms formed during this; series of reactions involving electron transport and ATP synthase that can trap energy and store it in ATP |
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Bioenergetics |
Study of the mechanisms of cellular energy release |
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Aerobic respiration |
ELECTRONS TRANSFERRED FROM GLUCOSE TO OXYGEN--Series of reactions (glycolysis, Krebs cycle, electron transport chain) that converts glucose to carbon dioxide, produces water, and generates energy-- final electron acceptor is oxygen-- used by chemoheterotrophs |
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Fermentation |
Oxygen not required and organic compounds are the final electron acceptors-- when oxygen levels are too low or an electron acceptor is unavailable, pyruvic acid is converted into lactic acid which allows ATP production
PRODUCES 2 ATP PER GLUCOSE= 4 ATP |
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Anaerobic respiration |
Involves same 3 pathways as aerobic but final electron acceptor is other oxidized ions such as NO3, SO4, CO2 |
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Glucose |
Starting compound-- superior electron donors (C6H12O6) |
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Glycolysis |
Converts glucose into pyruvic acid-- synthesizes ATP in the presence or absence of oxygen-- releases NADH-- GENERATES 2 ATPs, 2 PYRUVATES AND 2 NADH |
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Krebs cycle |
Mitochondrial matrix in eukaryotes and cytoplasm in bacteria-- converts pyruvic acid into acetyl coenzyme A, NADH released during this process and shuttled into electron transport and used to generate ATP via oxidative phosphorylation-- STARTS WITH ACETYL COENZYME A AND ENDS WITH OXALOACETATE PRODUCES 2 ATP AND 2 NADH |
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Electron transport chain |
Chain of special carriers that receive electrons from reduced carriers (NADH, FADH2) generated by glycolysis and Krebs cycle-- shuttles electrons through a series of redox transfers-- electrons accepted by hydrogen and water is produced-- PRODUCES 34 ATP |
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Cytochromes |
Involved in accepting and donating electrons to the next carrier in the series |
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Chemiosmosis |
Electron transport carriers shuttle electrons and actively pump hydrogen ions across membrane setting up a gradient of hydrogen ions-- happens in mitochondria |
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Proton motive force |
Consists of different charge between intermembrane (+) and matrix (-) Caused by chemiosmosis |
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ATP synthase |
Enzyme that has 2 motors: ion pump and enzyme thy can capture energy and store it as ATP-- consists of Fo and Fi |
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Fo |
rotates like a motor to pull in protons (in ATP synthase) |
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Fi |
pulls in ADP and phosphate groups-- forms and releases ATP |
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translocases |
on the mitochondrial membrane-- transport ATP out of mitochondria and ADP into it |
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Denitrification |
Enzymes can reduce nitrite to nitric oxide, nitrous oxide, and nitrogen gas (in anaerobic respiration) |
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Alcoholic fermentation |
Occurs in yeast or bacterial species that have metabolic pathways for converting pyruvic acid into ethanol |
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Acidic dermentation |
Reducing pyruvate to lactic acid |
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Mixed acid feementation |
Produces combination of acetic, lactic, succinic and formic acids |
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Amphibolism |
Property of a system to integrate catabolic and anabolic pathways to improve cell efficiency-- occurs during glycolysis and Krebs cycle |
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Gluconeogenesis |
Opposite of glycolysis-- turns pyruvic acid into glucose when there's inadequate glucose supply |
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Beta oxidation |
Fats can be degraded to acetyl and enter the Krebs cycle via acetyl coenzyme A |
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Amination |
Addition of an amino group to a carbon skeleton |
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Transamination |
Amino acids and carbohydrates interchanges |
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Deamination |
During times of carbohydrate deprivation, organisms can convert amino acids to intermediates of the Krebs cycle and derive energy from proteins-- results in formation of nitrogen waste products |
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What are the building blocks that make up macromolecules and organelles? |
Monosaccharides, amino acids, fatty acids, nitrogen bases and vitamins |
