Chapter Eight (quiz four) – Flashcards

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Metabolism
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all chemical reactions and physical work of the cell
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Functions of Metabolism
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1. Assembles smaller molecules into larger macro-molecules needed for the cell
2. Degrades macro-molecules into smaller molecules and yields energy
3. Energy is conserved into the form of ATP or HEAT
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Anabolism (biosynthesis)
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Any process that results in the synthesis of cell molecules and structures (usually requires energy input)
-making new molecule from existing parts
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Catabolism
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the breakdown of bonds of larger molecules into smaller molecules (often releases energy)
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Enzymes?
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are proteins that work as catalysts
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Catalysts
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chemicals that increas the rate of a chemical reaction without becoming part of the products of being consumed in the reaction
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What do catalysts do to activation engery
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lower it
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What is unique about each catalyst?
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unique characteristics such as shape, specificity and function
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Substrates?
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target molecule; each enzyme has a active site for these
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What are enzymes greatly effected by
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temperature and pH
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1st enzyme in glycolysis?
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Hexokinase
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Energy of Activation
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the amount of energy which must be overcome for a reaction to proceed
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How do enzymes promote a reaction?
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by serving as a PHYSICAL SITE upon which the reactant molecules (substrates) can be positioned for various interactions
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Enzyme-substrate interaction
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-for a reaction to take place, a temporary enzyme-substrate union must occur at the active site
-"lock and key" fit
-these bond are weak and easily reversible
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What is an ES complex?
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the enzyme and substrate bound together
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What are cofactors?
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supporting the work of enzymes
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Metallic cofactors?
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activate enzymess, help bring the active site and substrate close together, and participate directly in chemical reaction with the enzyme-substrate complex
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Coenzymes are?
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Organic compounds that work in conjunction with a apoenzyme to preform a necessary alteration of a substrate
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Coenzymes do?
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remove a chemical group from one substrate molecule and adds it to another substrate
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What is one of the most important components of coenzymes?
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VITAMINS
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Holoenzyme?
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apoenzyme (protein enzyme) + co-factor = holoenzyme = catalyzes actual function/reaction
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Classification of enzymes? (3 ways)
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1. Site of action
2. type of action
3. substrate in which they work with
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hydrolase (enzyme)
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breaks down lactose down into glucose and galatose
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hydrolyzes beta-lactam ring
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transferase (enzyme)
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synthesizes a strand of DNA using the complementary strand as a model
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oxidoreuctase (enzyme)
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catalyzes the conversion of pyuvric acid to lactic acid
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catalyzes the reduction 02
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Constitutive Enzymes?
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always present and in relatively constant amounts
(ex. enzymes of glycolysis)
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Regulated enzymes?
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Production is either induced or repressed in response to a change in the concentration of the substrate
(ex. lactose (lac) operon in E. coli)
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Lac operon in E. coli?
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the E. coli n the presence of lactose turns on its enzymes to break down lactose... regulated enzyme you fool!
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Dehydration recation
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water is one of the products
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Hydrolysis
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breaking down peptide bonds between amino acids. requires a water molecule that adds H and OH to the amino acids
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Virulence factors or toxins
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-unique exoenzymes that pathogens secrete
-these help them avoid host defenses or promote multiplication in tissues
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Labile enzymes?
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when enzymes are subjected to changes in normal conditions they become unstable or labile
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Denaturation?
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the weak bond that maintain the native shape of the apoenzyme are broken
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Enzymes that play a role in necessary molecular conversions by directing the transfer of function groups
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-aminotransferases
-phosphotransferases
-methyltransferases
-decarboxylases
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How do metabolic reactions usually occur?
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in a multi-series step or pathway
-each step is catalyzed by an enzyme
-each pathway has one or more enzyme pacemakers that set the rate of a pathway's progression
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What are intermedates in a metabolic pathway?
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Not the start or finished product... DUH
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Competitive inhibition?
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It is a direct control on the action of enzymes
-the cell supplies a molecule that resembles the enzyme's normal substrate, which then occupies and blocks the enzyme's active site
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Non-Competitive inhibition?
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direction controls on the action of enzymes
-the enzymes has TWO binding sites- the active site and the regulatory site; a regulator molecule binds to the regulatory site providing a negative feed back mechanism
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Enzyme Repression?
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Decrease enzyme expression (product goes back to DNA and says "ENOUGH!")
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Enzyme Induction?
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Increase enzyme expression (product goes back to DNA and says "MORE MORE")
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Exergonic Reactions?
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a reaction that releases energy as it goes forward: -delta G
usually catobolic RXNS
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Engergonic Reactions?
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a reaction that is driven forward with the addition of energy: +delta G
usually anabolic RXNS
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Redox reaction
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how biological systems extract energy, always occur in pairs (an electron donor paired with an electron acceptor
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Electron Carriers
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Repeatedly accept and release electrons and hydrogen
-some are coenzymes that transfer electrons and hyrogens
-ex. NAD, FAD, NADP
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ATP
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adenosine triphosphate
-Metabolic Money
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ATP molecular structure
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-nitrogen base
-5 carbon sugar
-chain of three phosphate group
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How does ATP yield energy
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breaking of bonds between two phosphates of ATP yeilds ADP plus the inorganic phosphate
-the most energy comes from breaking the 3rd group
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how much energy comes from ATP
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-7.3 kcal/mol
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Substrate Level Phosphorylation
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phosphate off substrate to ATP OR the transfer of phosphate group
- phosphoenolpyruvate+ADP -> pyruvate+ATP
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What is a pathway?
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a series of biochemical reactions
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what is often the nutrient going through catabolism?
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glucose!
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What are the three major catabolism pathways?
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1. Aerobic respiration
2. Fermentation
3. Anaerobic Respiration
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Aerobic Respiration?
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series of reactions that convert glucose to CO2 and allows the cell to recover significant amounts of energy; requires OXYGEN (makes water)
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Fermentation?
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use only glycolysis to incompletely oxidize glucose
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Anaerobic respiration?
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does not use molecular oxygen as the final acceptor
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Anaerobic random ifo
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-its a series of enzyme-catalyzed reactions
-electrons are transfered from fuel molecules to oxygen as a final electron acceptor
-provides ATP and metabolic intermediates for many other pathways
-glucose is the starting compound
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What does glycolysis convert glucose to?
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it goes through several steps into pyruvic acid OR pyruvavte
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3 phases of glycolsis
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1st phase: 2 ATP taken in
2nd phase: 2 three carbon molecules made
3rd phase: making 4 ATP and 2 NADH
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Products of Glycolysis
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-2 pyruvate molecules (can under go more catabolic RNX to extract more energy)
-2 ATP
-2 NADH
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What does Glycolysis convert glucose into?
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Pyruvate
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3 phases of pyruvate
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1st: 2 atp taken in
2nd: 2 three carbon molecules made
3rd: making 4 atp and 2 nadh
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Products of Glycolysis
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2 pyruvate molecules
2 ATP
2 NADH
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What does pyruvic acid serve as?
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an important position in several pathways
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Krebs Cycle take place where?
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in the cytoplasm of bacteria and mitochondrial matrix in eukaryotes
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Products of krebs cycle?
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1 glucose molecule makes 2 pyruvate
each pyruvate makes: 3 CO2, 4 NADH, 1 FADH2, 1 ATP
so total
8 NADH
2 FADH2
2 ATP
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After Krebs cycle what is up with glucose?
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It has now be completely oxidized to carbon dioxide
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What is the final processing mill
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electron transport chain
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What do electrons pass through in the electron transport chain?
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membrane carries called CYTOCHROMES
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How is atp formed in electron transport chain
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the protons pass through ATP synthase to form ATP

this is an endergonic reaction-- energy comes from protons moving down the gradient
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1 FADH2 = _____ ATP
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2
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1 NADH = ____ ATP
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3
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Aerobic respiration yields....?
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36-38 ATP per gulcose
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Anaerobic respiration
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functions like aerobic system except it utilizes oxygen-containing ions rather than free oxygen as the final electron acceptor
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Anaerobic Respiration yield?
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2-36 ATP
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Fermentation is..?
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the incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
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What does fermentation use as the terminal electron acceptor
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organic compounds
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How are bacteria able to grow as fast using fermentation as they would in the presence of O2
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they increase the rate of glycolysis.. the 2 ATP build up
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Products of fermentation?
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alcoholic beverages, organic acids, dairy products, vitamins, antobiotics
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Two general categories of fermentation?
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1. Alcoholic fermentation
2. Acidic Fermentation
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Commonality between Alcoholic and Acidic Fermentation
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NADH getting reformed into NAD... this allows glycolysis to continue
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Alcoholic fermentation products
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ethanol, CO2 and NAD
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Acidic Fermentation products
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varied... but always lactic acid
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lactic acid bacteria fermentation product
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they ferment pyruvate and reduce it to lactic acid (occurs in our muscles)
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Heterolactic fermentation
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when glucose is fermented to a mixture of lactic acid, acetic acid, carbon dioxide and NAD
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Mixed acid fermentation
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Produced a combination of acetic, lactic, succinic and formic acids and lowers the pH of a medium to about 4
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homolactic bacteria?
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S. coccus or latobacilus form lacti acid... souring of milk
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Amphibolism
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The property of a system to integrate catabolic and anabolic pathways to improve cell efficiency
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where do monosaccharides, amino acids, fatty acids, nitrogen bases and vitamins come from (in regards to anabolism)
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1. enter the cell from outside as nutrients
2. Can be synthesized through various cellular pathways
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Amino acids, protein synthesis and nucleic acid synthesis?
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some organisms can synthesize all 20 amino acids
other organisms (especially animals) must acquire the essential ones from their diets
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Assembly of the cell
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when anabolism produces enough macro-molecules to serve two cells, then the cell undergoes binary fisson
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