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BL 616 Test 2 study guide. The test will probably have 25 multiple choice, and about 10 problems with short
answers; maybe a passage(s) to read and several questions to answer, structures to draw. Look between the
different chapters, not just each alone. Read the PowerPoint slides, paying attention to the Learning Outcomes,
and major points emphasized. Review the questions at the ends of the chapters, and problems discussed during
the chapters, and also including the major patients who were discussed.
Section four – fuel oxidation and the generation of ATP – general principles
Describe the different pathways and their intersections – fatty acid oxidation and glycolysis both feed into the
TCA and oxidative phosphorylation (electron transport chain, ETC).
Describe how ATP is used to power energy-requiring reactions
Describe the regulation of pathways, and what determines which paths are used – relevant hormones, energy
state of cell, NADH/NAD+, ATP/ADP etc
Describe the relative energy yields (using the 3 ATP per NADH in ETC, and 2 ATP per FAD(2H) in ETC) for
fatty acid oxidation vs. glucose oxidation vs. anaerobic glycolysis
Oxidation/ reduction reactions: what happens to the compound getting oxidized, and what happens to the
compound getting reduced? Diagram some specific examples.
Diagram a cell with mitochondrion and peroxisome, and indicate where different major enzyme systems are
locate, and on what surface of which membranes, and the H+ gradient.
What are the functions of the plasma membrane, the peroxisome, the mitochondrion, and the respiratory burst in
immune cells for the phagosome?
Describe the relevance of oxygen, as necessary for maximum energy yield, but toxic as well.
Explain yield from aerobic path for glucose vs. anaerobic (fermentation); yeast vs. human cells.
Describe the fed state with lots of glucose vs. fasting state, and mobilization of fatty acids and ketone bodies.
Enzymology: what are different classes of enzymes and what types of reactions do they do?
Oxidases, oxygenases, peroxidases, thiolases, dehydrogenases, carboxylases. Kinases, SOD, catalase
Phosphoglucomutase, Synthases vs. synthetases, ATP synthase
Describe unusual enzymes: pyruvate dehydrogenase complex (PDC), the -ketoacid dehydrogenase complex
and their regulation
What are isozymes and some examples
Coenzymes: Describe FAD vs. NADH, and what is similar, what is different? What types of enzymes are they
normally associated?
Structures of major macromolecules – be able to draw a generic nucleotide, fatty acid (saturated and
unsaturated), triacylglycerol, glucose, glucose-1-phosphate vs glucose-6-phosphate, ATP, NAD, CoASH,
Pyruvate, lactate, acetyl-CoA, acetoacetate ketone body, glutathione
Small molecules are important: role of Ca2+, role of Fe2+,
Abbreviations: TCA, ETC, TPP, SOD, d
Compounds that sound similar: creatine vs. carnitine,
Na+/K+ ATPase
Ch 19 overview of metabolism, bioenergetics
Thermodynamics tells what is possible, relates to concentrations of substrate, lproduct
Also whether exogonic, endergonic reaction
Coupling of ATP hydrolysis to permit biosynthetic (endergonic) reactions
Relative costs of synthesizing glycogen from glucose, vs. oxidation of glucose
UDP-glucose is intermediate in glycogen synthesis
Calorie content of foods – why glucose vs. fatty acids differ
Where is most of the oxygen used?
Ch 20 TCA cycle – needs oxygen
Describe basic TCA cycle: what goes in, what initial product, what is formed (GTP, NADH, FAD(2H), CO2
and how many of each; what final product. (Fig. 3)
Describe other functions of the intermediates in the cycle – biosynthesis, breakdown of amino acids, fatty acids,
etc; many fuels feed into Acetyl CoA (Fig. 19)
Energetics of TCA cycle
**Regulation of TCA cycle (figs. 12, 17); PDC Fig. 15
New terms: anaplerotic
How do the mitochondrial enzymes get there – what is made in mitochondria vs. nuclear-encoded?
Ch 21 oxidative phosphorylation requires oxygen
Describe basic process of NADH, FAD(2H) donating e- to O2 -> H2O; mitochondria
ATP synthase makes ATP; where is proton gradient, chemiosmotic mechanism
Complications of interference with ETC – cyanide, OXPHOS diseases, anemia
Names of the complexes: NADH dehydrogenase ND1
Succinate dehydrogenase complex II, coenzyme Q, cytochromes, and cytochrome C oxidase
OXPHOS diseases MERFF, LHON
Uncoupling agents DNP, thermogenin
Differential transport across inner and outer membranes of mitochondrion
Ch 22 glycolysis
Describe basic process – what starts, what ATP needed, what ending and what energy yield
Two phases: preparation, and energy generating; what compartment in cell?
Critical enzymes: hexokinase (glucokinase in liver), phosphofructokinase-1 (PFK-1), pyruvate kinase, pyruvate
dehydrogenase, and regulation
Pyruvate as critical point – availability of oxygen determine next steps; lactic acidosis
Shuttle for NADH into mitochondrion
Glycolysis generates precursors for other paths
Ch 23 oxidation of fatty acids, ketones
Oxidation of long-chain fatty acids (LCFA) – from absorption or degradation from adipose tissue to liver…
Role of CoASH and of carnitine; describe cycles of -oxidation, need for ATP at beginning, what are
products at end from typical LCFA? Role of oxygen?
Fatty acids used as fuels and when, which are most common FA?
Acyl CoA synthetases specificity for chain length FA
Energy yield from fatty acid oxidation
Synthesis of ketone bodies by liver, use by other tissues
Ch 24 reactive oxygen species
Describe major forms of ROS, superoxide, hydrogen peroxide, hydroxyl radical and how they are formed.
Role of accidental CoQH, metals, radiation,
Describe toxic effects of ROS on cell components – different parts of cell
Lipid peroxidation free radical chain reaction destroys membranes, ROS effects on DNA
NO signal molecule and toxic; RNOS
Respiratory burst by phagocytic cells
Cell defenses against ROS, RNOS – enzymes, antioxidants, compartmentalization
Vitamin E, vitamin C, glutathione, SOD, catalase, peroxidase,