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ACS Biochemistry Final Exam 2024: Complete 200 Questions with Detailed Answers, Exams of Biochemistry

A comprehensive set of 200 questions and answers covering various topics in biochemistry, including carbohydrates, lipids, proteins, nucleic acids, and cellular respiration. It is designed to help students prepare for their final exam in acs biochemistry. Detailed explanations for each answer, making it a valuable resource for understanding key concepts and reinforcing learning.

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2024/2025

Available from 11/08/2024

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Download ACS Biochemistry Final Exam 2024: Complete 200 Questions with Detailed Answers and more Exams Biochemistry in PDF only on Docsity! 1 | P a g e ACS BIOCHEMISTRY FINAL EXAM 2024 ACTUAL EXAM COMPLETE 200 QUESTIONS WITH DETAILED VERIFIED ANSWERS (100% CORRECT ANSWERS) ALREADY GRADED A+ What is the D configuration of a sugar in a Fisher projection? - CORRECT ANSWER >>>>chyrolcarbon furthest from the carboxyl group hydroxyl on right What is the L configuration of a sugar in a Fisher projection? - CORRECT ANSWER >>>>hydroxyl on left What is the difference between glycogen and amylopectin? - CORRECT ANSWER >>>>glycogen- has branches about every 10 residues (more highly branched) 2 | P a g e amylopectin- has branches about every 25 What is amylose made up of? - CORRECT ANSWER >>>>glucose What makes up starch? - CORRECT ANSWER >>>>amylose amlyopectin What is a glycosidic bond? - CORRECT ANSWER >>>>links two monosaccharides together at points 1 and 4 What is the difference between an alpha(1-4) and beta(1-4) linkage? - CORRECT ANSWER >>>>alpha: when the oxygen is pointed down in a glycosidic bond beta: when the oxygen is pointed up in a glycosidic bond 5 | P a g e Why type of amino acid is present in the plasma membrane among the fatty acid tails? - CORRECT ANSWER >>>>hydrophobic/nonpolar What is passive transport (simple diffusion)? - CORRECT ANSWER >>>>no energy required no protein required move from high concentration to low concentration water, gases, ethanol (small nonpolar) can pass through What is facilitated diffusion? - CORRECT ANSWER >>>>requires protein no energy required molecules are two large to go through on their own 6 | P a g e What is active transport? - CORRECT ANSWER >>>>energy is required moves from low to high concentration How many carbon atoms do most fatty acids have? - CORRECT ANSWER >>>>even number What bond holds nucleotides together? - CORRECT ANSWER >>>>phosphodiester bond What base pairing exists in nucleic acids? How many hydrogen bonds between them? - CORRECT ANSWER >>>>G--C (3 hydrogen bonds) A--T (2 hydrogen bonds) What is the first amino acid always placed in a protein? - CORRECT ANSWER >>>>methionine (Met) start codon 7 | P a g e What 3 things make up a nucleotide? - CORRECT ANSWER >>>>nitrogen base phosphate group pento-sugar (ribose or deoxyribose) What are the 3 main differences between DNA and RNA? - CORRECT ANSWER >>>>RNA single strand DNA is double stranded RNA has uracil DNA has thiamine RNA has ribose DNA has deoxyribose What part of the structure makes DNA such a stable molecule? - CORRECT ANSWER >>>>very polar sugar phosphate backbound the bases are stacked in the interior that are nonpolar 10 | P a g e What is an allosteric enzyme? - CORRECT ANSWER >>>>there are two bonding sites (active site and another) What do enzymes do? - CORRECT ANSWER >>>>catalyze a reaction What enzyme forms a bond between four molecules? - CORRECT ANSWER >>>>ligase How do enzymes work? - CORRECT ANSWER >>>>lower the activation energy to catalyze the reaction What is enzyme cooperativity? - CORRECT ANSWER >>>>when one subunit binds oxygen, it changes shape and makes it more likely for the other subunit What is the difference between competitive and noncompetitive inhibitors? - CORRECT 11 | P a g e ANSWER >>>>competitive inhibitor: substrate and inhibitor compete to bind with the active site noncompetitive inhibitor: inhibitor binds to allosteric site instead of active site but enzyme can't also bind What is oxidation and reduction? - CORRECT ANSWER >>>>reduction: add hydrogen to result in a higher chemical potential oxidation: When you have a hydrolysis of bonds in food, what does that do? - CORRECT ANSWER >>>>releases energy What reaction breaks bonds within cells? - CORRECT ANSWER >>>>hydrolysis 12 | P a g e When a reaction breaks bonds within cells, does this reaction require or release energy? - CORRECT ANSWER >>>>releases energy How does the reaction that breaks bonds within cells relate to delta G? - CORRECT ANSWER >>>>energy is used to build the bonds the delta G becomes negative when energy is released What factors affect enzyme activity? - CORRECT ANSWER >>>>pH heat What process results in the anabolism of glucose? - CORRECT ANSWER >>>>hydrolysis of the anhydride bonds provide energy for anabolism What is the main function of NADH within cellular respiration? - CORRECT ANSWER 15 | P a g e Henderson-Hasselbach Equation - CORRECT ANSWER >>>>pH = pKa + log ([A-] / [HA]) FMOC Chemical Synthesis - CORRECT ANSWER >>>>Used in synthesis of a growing amino acid chain to a polystyrene bead. FMOC is used as a protecting group on the N-terminus. Salting Out (Purification) - CORRECT ANSWER >>>>Changes soluble protein to solid precipitate. Protein precipitates when the charges on the protein match the charges in the solution. Size-Exclusion Chromatography - CORRECT ANSWER >>>>Separates sample based on size with smaller molecules eluting later. Ion-Exchange Chromatography - CORRECT ANSWER >>>>Separates sample based on 16 | P a g e charge. CM attracts +, DEAE attracts -. May have repulsion effect on like charges. Salt or acid used to remove stuck proteins. Hydrophobic/Reverse Phase Chromatography - CORRECT ANSWER >>>>Beads are coated with a carbon chain. Hydrophobic proteins stick better. Elute with non-H-bonding solvent (acetonitrile). Affinity Chromatography - CORRECT ANSWER >>>>Attach a ligand that binds a protein to a bead. Elute with harsh chemicals or similar ligand. SDS-PAGE - CORRECT ANSWER >>>>Uses SDS. Gel is made from cross-linked polyacrylamide. Separates based off of mass with smaller molecules moving faster. Visualized with Coomassie blue. 17 | P a g e SDS - CORRECT ANSWER >>>>Sodium dodecyl sulfate. Unfolds proteins and gives them uniform negative charge. Isoelectric Focusing - CORRECT ANSWER >>>>Variation of gel electrophoresis where protein charge matters. Involves electrodes and pH gradient. Protein stops at their pI when neutral. FDNB (1-fluoro-2,3-dinitrobenzene) - CORRECT ANSWER >>>>FDNB reacts with the N-terminus of the protein to produce a 2,4-dinitrophenol derivative that labels the first residue. Can repeat hydrolysis to determine sequential amino acids. DTT (dithiothreitol) - CORRECT ANSWER >>>>Reduces disulfide bonds. 20 | P a g e Parallel ß-sheet - CORRECT ANSWER >>>>Same sheet directions (C & N-termini line up). Has angled H-bonds. ß-turns - CORRECT ANSWER >>>>Tight u-turns with specific phi-psi angles. Must have gly at position 3. Proline may also be at ß-turn because it can have a cis-omega angle. Loops - CORRECT ANSWER >>>>Not highly structured. Not necessary highly flexible, but can occasionally move. Very variable in sequence. Circular Dichroism - CORRECT ANSWER >>>>Uses UV light to measure 2° structure. Can be used to measure destabilization. Disulfide-bonds - CORRECT ANSWER >>>>Bonds between two -SH groups that form between 2° and 3° structure. 21 | P a g e ß-mercaptoethanol - CORRECT ANSWER >>>>Breaks disulfide bonds. α-keratin - CORRECT ANSWER >>>>formed from 2 α-helices twisted around each other. "Coiled coil". Cross-linked by disulfide bonds. Collagen - CORRECT ANSWER >>>>Repeating sequence of Gly-X-Pro. 3 stranded "coiled coil". Contains gly core. Myoglobin 4° Structure - CORRECT ANSWER >>>>Symmetric homodimer, Hemoglobin 4° Structure - CORRECT ANSWER >>>>Tetramer. Dimer of dimers. α2ß2 tetramer. α/ß Protein Folding - CORRECT ANSWER >>>>Less distinct areas of α and ß folding. 22 | P a g e α+ß Protein Folding - CORRECT ANSWER >>>>Two distinct areas of α and ß folding. Mechanism of Denaturants - CORRECT ANSWER >>>>Highly soluble, H-binding molecules. Stabilize protein backbone in water. Allows denatured state to be stabilized. Temperature Denaturation of Protein - CORRECT ANSWER >>>>Midpoint of reaction is Tm. Cooperative Protein Folding - CORRECT ANSWER >>>>Folding transition is sharp. More reversible. Folding Funnel - CORRECT ANSWER >>>>Shows 3D version of 2D energy states. Lowest energy is stable protein. Rough funnel is less cooperative. 25 | P a g e O2 Binding Event - CORRECT ANSWER >>>>O2 binds to T-state and changes the heme to R- state. Causes a 0.4Å movement of the iron. Hemoglobin Binding Curve - CORRECT ANSWER >>>>4 subunits present in hemoglobin that can be either T or R -state. Cooperative binding leads to a sigmoidal curve. Binding Cooperativity - CORRECT ANSWER >>>>When one subunit of hemoglobin changes from T to R-state the other sites are more likely to change to R-state as well. Leads to sigmoidal graph. Homotropic Regulation of Binding - CORRECT ANSWER >>>>Where a regulatory molecule is also the enzyme's substrate. Heterotropic Regulation of Binding - CORRECT ANSWER >>>>Where an allosteric regulator is present that is not the enzyme's substrate. 26 | P a g e Hill Plot - CORRECT ANSWER >>>>Turns sigmoid into straight lines. Slope = n (# of binding sites). Allows measurement of binding sites that are cooperative. pH and Binding Affinity (Bohr Affect) - CORRECT ANSWER >>>>As [H+] increases, Histidine group in hemoglobin becomes more protonated and protein shifts to T-state. O2 binding affinity decreases. CO2 binding in Hemoglobin - CORRECT ANSWER >>>>Forms carbonic acid that shifts hemoglobin to T-state. O2 binding affinity decreases. Used in the peripheral tissues. BPG (2,3-bisphosphoglycerate) - CORRECT ANSWER >>>>Greatly reduces hemoglobin's affinity for O2 by binding allosterically. Stabilizes T-state. Transfer of O2 can improve 27 | P a g e because increased delivery in tissues can outweigh decreased binding in the lungs. Michaelis-Menton Equation - CORRECT ANSWER >>>>V0 = (Vmax[S]) / (Km + [S]) Km in Michaelis-Menton - CORRECT ANSWER >>>>Km = [S] when V0 = 0.5(Vmax) Michaelis-Menton Graph - CORRECT ANSWER >>>> Lineweaver-Burke Graph - CORRECT ANSWER >>>>Slope = Km/Vmax Y-intercept = 1/Vmax X-intercept = - 1/Km Lineweaver-Burke Equation - CORRECT ANSWER >>>>Found by taking the reciprocal of the Michaelis-Menton Equation. 30 | P a g e Mutarotation - CORRECT ANSWER >>>>Conversion from α to ß forms of the sugar at the anomeric carbon. Anomeric Carbon - CORRECT ANSWER >>>>Carbon that is cyclized. Always the same as the aldo or keto carbon in the linear form. α vs. ß sugars - CORRECT ANSWER >>>>α form has -OR/OH group opposite from the -CH2OH group. ß form has -OR/OH group on the same side as the -CH2OH group. Starch - CORRECT ANSWER >>>>Found in plants. D-glucose polysaccharide. "Amylose chain". Unbranched. Has reducing and non- reducing end. Amylose Chain - CORRECT ANSWER >>>>Has α- 1,4-linkages that produce a coiled helix similar 31 | P a g e to an α-helix. Has a reducing and non-reducing end. Amylopectin - CORRECT ANSWER >>>>Has α- 1,4-linkages. Has periodic α-1,6-linkages that cause branching. Branched every 24-30 residues. Has reducing and non-reducing end. Reducing Sugar - CORRECT ANSWER >>>>Free aldehydes can reduce FeIII or CuIII. Aldehyde end is the "reducing" end. Glycogen - CORRECT ANSWER >>>>Found in animals. Branched every 8-12 residues and compact. Used as storage of saccharides in animals. Cellulose - CORRECT ANSWER >>>>Comes from plants. Poly D-glucose. Formed from ß-1,4- linkage. Form sheets due to equatorial -OH groups that H-bond with other chains. 32 | P a g e Chitin - CORRECT ANSWER >>>>Homopolymer of N-acetyl-ß-D-glucosamine. Have ß-1,4- linkages. Found in lobsters, squid beaks, beetle shells, etc. Glycoproteins - CORRECT ANSWER >>>>Carbohydrates attached to a protein. Common outside of the cell. Attached at Ser, Thr, or Asn residues. Membrane Translayer Flip-Flop - CORRECT ANSWER >>>>Typically slow, but can be sped up with Flippase, Floppase, or Scramblase. Membrance Fluidity - CORRECT ANSWER >>>>Membrane must be fluid. Cis fats increase fluidity, trans fats decrease fluidity. Type I Integral Membrane Protein - CORRECT ANSWER >>>>Membrane protein with C- terminus inside and N-terminus outside 35 | P a g e A-form DNA - CORRECT ANSWER >>>>Condensed form of DNA. Deeper major groove and shallower minor groove. B-form DNA - CORRECT ANSWER >>>>Watson- Crick model DNA. Deep, wide major groove. Z-form DNA - CORRECT ANSWER >>>>Left- handed helical form of DNA Inverted Repeat in DNA - CORRECT ANSWER >>>>Found in double-strands. TTAGCAC|GTGCTAA AATCGTG|CACGATT Forms a cruciform. Mirror Repeat in DNA/RNA - CORRECT ANSWER >>>>Found in single-strands. TTAGCAC|GTGCTAA Forms a hairpin 36 | P a g e DNA UV Absorbtion - CORRECT ANSWER >>>>Absorbs UV light at 260nm. Restriction Enzyme - CORRECT ANSWER >>>>Cuts DNA at specific restriction sites. DNA Base-paring - CORRECT ANSWER >>>>G-C base pairs have 3 H-bonds A-T base pairs have 2 H-bonds GPCR (G-protein coupled receptor) - CORRECT ANSWER >>>>α-helical integral membrane proteins. Is a αßɣ heterotrimer. ß-adrenergic receptor - CORRECT ANSWER >>>>Prototype for all GPCR's. Bind adrenaline/epinephrine to stimulate breakdown of glycogen. Step 1 of Epinephrine Signal Transduction - CORRECT ANSWER >>>>Epinephrine binds to its specific receptor 37 | P a g e Step 2 of Epinephrine Signal Transduction - CORRECT ANSWER >>>>Hormone complex causes GDP bound to α-subunit to be replaced by GTP, activating α-subunit Step 3 of Epinephrine Signal Transduction - CORRECT ANSWER >>>>Activated α-subunit separates from ßɣ-complex and moves to adenylyl cyclase, activating it. Step 4 of Epinephrine Signal Transduction - CORRECT ANSWER >>>>Adenylyl cyclase catalyzes the formation of cAMP from ATP Step 5 of Epinephrine Signal Transduction - CORRECT ANSWER >>>>cAMP phosphorylates PKA, activating it Step 6 of Epinephrine Signal Transduction - CORRECT ANSWER >>>>Phosphorylated PKA 40 | P a g e NADH - CORRECT ANSWER >>>> FADH2 - CORRECT ANSWER >>>>Single-electron transfer NADPH - CORRECT ANSWER >>>> FMN - CORRECT ANSWER >>>>Single electron transfer. Step 1 of Glycolysis - CORRECT ANSWER >>>>Glucose --> Glucose 6-phosphate. Uses hexokinase enzyme. ATP --> ADP Step 2 of Glycolysis - CORRECT ANSWER >>>>Glucose 6-phosphate <--> Fructose 6- phosphate Uses phosphohexose isomerase enzyme. 41 | P a g e Step 3 of Glycolysis - CORRECT ANSWER >>>>Fructose 6-phosphate --> Fructose 1,6- bisphosphate Uses PFK-1 (phosphofructokinase-1) enzyme. ATP --> ADP First Committed Step of Glycolysis - CORRECT ANSWER >>>>Step 3 of Glycolysis. Fructose 6-Phosphate --> Fructose 1,6- bisphosphate. (PFK-1) Step 4 of Glycolysis - CORRECT ANSWER >>>>Fructose 1,6-bisphosphate <--> dihydroxyacetone + glyceraldehyde 3- phosphate. Uses aldolase enzyme. Step 5 of Glycolysis - CORRECT ANSWER >>>>Dihydroxyacetonephosphate <--> glyceraldehyde 3-phosphate Uses triose phosphate isomerase enzyme. 42 | P a g e Step 6 of Glycolysis - CORRECT ANSWER >>>>Glyceraldehyde 3-Phosphate + Pi <--> 1,3- biphosphoglycerate. Uses G3P dehydrogenase enzyme. NAD+ <--> NADH First Energy Yielding Step of Glycolysis - CORRECT ANSWER >>>>Step 6 of Glycolysis. G3P + Pi <--> 1,3-bisphosphoglycerate Step 7 of Glycolysis - CORRECT ANSWER >>>>1,3-bisphosphoglycerate + ADP <--> 3- phosphoglycerate + ATP Uses phosphoglycerate kinase enzyme. First ATP Yielding Step of Glycolysis - CORRECT ANSWER >>>>Step 7 of Glycolysis. 1,3-bisphosphoglycerate <--> 3- phosphoglycerate Step 8 of Glycolysis - CORRECT ANSWER >>>>3- phosphoglycerate <--> 2-phosphoglycerate 45 | P a g e TPP Cofactor - CORRECT ANSWER >>>>Common acetaldehyde carrier. Used in pyruvate decarboxylase, pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, and transketolase Bypass Reactions in Gluconeogenesis - CORRECT ANSWER >>>>Steps 1,3, and 10 must be bypassed. Gluconeogenic Bypass of Step 10 - CORRECT ANSWER >>>>Bicarbonate + Pyruvate --> Oxaloacetate Pyruvate decarboxylate (biotin) ATP --> ADP Oxaloacetate --> PEP PEP carboxykinase GTP --> GDP + CO2 46 | P a g e Gluconeogenic Bypass of Step 3 - CORRECT ANSWER >>>>Fructose 1,6-bisphosphate + H2O --> Fructose 6-phosphate + Pi Uses FBPase-1 (coordinated with PFK-1) Gluconeogenic Bypass of Step 1 - CORRECT ANSWER >>>>Glucose 6-phosphate + H2O --> Glucose + Pi Uses glucose 6-phosphatase. Cost of Gluconeogenesis - CORRECT ANSWER >>>>4 ATP, 2 GTP, and 2 NADH Oxidative Pentose Phosphate Pathway - CORRECT ANSWER >>>>Uses glucose 6- phosphate to produce 2 NADPH and ribose 5- phosphate used for biosynthesis Non-Oxidative Pentose Phosphate Pathway - CORRECT ANSWER >>>>Regenerates glucose 6- phosphate from ribose 5-phosphate. Uses transketolase and transaldolase enzymes. 47 | P a g e Transketolase - CORRECT ANSWER >>>>Transfers a two-carbon keto group Transaldolase - CORRECT ANSWER >>>>Transfers a three-carbon aldo group Enzyme Km and Substrate Concentration - CORRECT ANSWER >>>>Most enzymes have a Km that is near the concentration of the substrate. Fructose 2,6-bisphosphate - CORRECT ANSWER >>>>Not a glycolytic intermediate. Interconverts between fructose 2,6- bisphosphate and fructose 6-phosphate using PFK-2 and FBPase-2 Regulation with fructose 2,6-bisphosphate - CORRECT ANSWER >>>>Activates PFK-1 encouraging glycolysis. Inhibits FBPase-1 discouraging gluconeogenesis 50 | P a g e Uses isocitrate dehydrogenase NAD(P)+ --> NAD(P)H + CO2 Step 4 of the Citric Acid Cycle - CORRECT ANSWER >>>>α-ketoglutarate --> succinyl-CoA Uses α-ketoglutarate dehydrogenase complex CoA + NAD+ --> NADH + CO2 Step 5 of the Citric Acid Cycle - CORRECT ANSWER >>>>Succinyl-CoA <--> Succinate Uses succinyl-CoA synthetase enzyme GDP + Pi <--> GTP + CoA Step 6 of the Citric Acid Cycle - CORRECT ANSWER >>>>Succinate <--> Fumarate Uses succinate dehydrogenase FAD <--> FADH2 Step 7 of the Citric Acid Cycle - CORRECT ANSWER >>>>Fumarate <--> L-Malate Uses fumarase enzyme 1) OH- 2) H+ --> 51 | P a g e Step 8 of the Citric Acid Cycle - CORRECT ANSWER >>>>L-Malate <--> Oxaloacetate Uses malate dehydrogenase enzyme NAD+ <--> NADH Net Energy Gain of the Citric Acid Cycle - CORRECT ANSWER >>>>3 NADH, FADH2, and GTP NADH Producing Steps of the Citric Acid Cycle - CORRECT ANSWER >>>>Steps 3, 4, and 8. Isocitrate --> α-ketoglutarate α-ketoglutarate --> Succinyl-CoA L-Malate --> Oxaloacetate FADH2 Producing Steps of the Citric Acid Cycle - CORRECT ANSWER >>>>Step 6 Succinate <--> Fumarate Using succinate dehydrogenase enzyme 52 | P a g e GTP/ATP Producing Steps of the Citric Acid Cycle - CORRECT ANSWER >>>>Step 5 Succinyl-CoA <--> Succinate Using succinyl-Coa synthetase CO2 Producing Steps of the Citric Acid Cycle - CORRECT ANSWER >>>>Steps 3 and 4 Isocitrate --> α-ketoglutarate α-ketoglutarate --> Succinyl-CoA Biotin Structure - CORRECT ANSWER >>>> Biotin Function - CORRECT ANSWER >>>>Prosthetic group that serves as a CO2 carrier to separate active sites on an enzyme Regulation of the Citric Acid Cycle - CORRECT ANSWER >>>>Regulation occurs at Steps 1, 2, 4, and 5. High energy molecules (ATP, Acetyl-CoA, NADH) inhibit while low-energy molecules (ADP, AMP, CoA, NAD+) activate these steps 55 | P a g e Step 4 of ß-oxidation - CORRECT ANSWER >>>>ß-ketoacyl-CoA (+ CoA) --> Fatty acyl-Coa (shorter) Uses thiolase enzyme ß-oxidation in plants - CORRECT ANSWER >>>>Electrons are passed directly to molecular oxygen releasing heat and H2O2 instead of the respiratory chain. ω-oxidation - CORRECT ANSWER >>>>Similar to ß-oxidation but occurs simultaneously on both ends of the molecule. α-oxidation - CORRECT ANSWER >>>>Form of oxidation of branched FA's. Produced propionyl-CoA that must be converted to succinyl-CoA for use in the CAC Ketone bodies - CORRECT ANSWER >>>>Consists of Acetoacetate, Acetone, and D- ß-hydroxybutryate. 56 | P a g e Formation begins from condensation of 2 acetyl-CoA --> Acetoacetyl-CoA (+ CoA) D-ß-hydroxybutryate can be broken into 2 acetyl-CoA and used as fuel. Zymogen - CORRECT ANSWER >>>>An inactive precursor of an enzyme, activated by various methods (acid hydrolysis, cleavage by another enzyme, etc.) PLP Structure - CORRECT ANSWER >>>> Amidotransferase - CORRECT ANSWER >>>>Uses a PLP group to transfer amino group from an amino acid to α-ketoglutarate to form L-glutamate and an α-ketoglutarate. Ammonia (NH4+) Transportation - CORRECT ANSWER >>>>L-glutamate is converted to L- glutamine via glutamine synthetase. ATP + NH4+ --> ADP + Pi 57 | P a g e L-glutamine can be converted back to L- glutamate in the liver. Glucose-Alanine Cycle - CORRECT ANSWER >>>>Pyruvate can be converted into Alanine via alanine aminotransferase (PLP). Adds a NH4+ group from glutamate to pyruvate. Alanine can travel to the liver and be reconverted back into pyruvate needed for gluconeogenesis. Production of carbamoyl-phosphate - CORRECT ANSWER >>>>NH4+ --> Carbamoyl Phosphate Produced by carbamoyl phosphate synthetase I 2 ATP + HCO3 --> 2ADP + Pi Step 1 of the Urea Cycle - CORRECT ANSWER >>>>Ornithine (+ carbamoyl phosphate) --> citrulline Uses ornithine transcarbamoylase enzyme Only step to occur in the mitochondria 60 | P a g e pKa of Tyrosne R-group - CORRECT ANSWER >>>>10 FAD Structure - CORRECT ANSWER >>>> Q (Ubiquinone/Coenzyme Q) Structure - CORRECT ANSWER >>>> Q (Ubiquinone/Coenzyme Q) Function - CORRECT ANSWER >>>>Lipid soluble electron carrier. Carries 2 electrons with 2 H+. ETC (Electron Transport Chain) - CORRECT ANSWER >>>>Consists of 4 functional protein complexes. Complex I in the ETC - CORRECT ANSWER >>>>Accepts two electrons from NADH via an FMN cofactor. Transfers 4H+ to Pside and 2H+ to Q 61 | P a g e Complex II in the ETC - CORRECT ANSWER >>>>Succinate dehydrogenase. Accepts two electrons electrons from succinate via an FAD group. Q --> QH2 Complex III in the ETC - CORRECT ANSWER >>>>Transfers two electrons from QH2 to cytochrome c via the Q-cycle. Transfers 4H+ to Pside. Complex IV in the ETC - CORRECT ANSWER >>>>Transfers electrons from cytochrome c to O2. Four electrons are used to reduce on O2 into two H2O molecules. Transfers 4H+ to Pside Mitochondrial ATP Synthase - CORRECT ANSWER >>>>Consists of F1 and F0 domains F1 Domain of Mitochondrial ATP Synthase - CORRECT ANSWER >>>>Hexamer of 3 αß dimers. Catalyze ADP + Pi --> ATP via binding- change model 62 | P a g e F0 Domain of Mitochondrial ATP Synthase - CORRECT ANSWER >>>>Causes rotation of γ- subunit via a half channel and H+ gradient Malate-Aspartate Shuttle - CORRECT ANSWER >>>>Used to maintain gradient of NADH inside of the mitochondria. Involves transport of malate or aspartate; aspartate aminotransferase; and malate dehydrogenase. RuBisCo (Ribulose 1,5-bisphosphate carboxylase/oxygenase) - CORRECT ANSWER >>>>Incorporates CO2 into ribulose 1,5- bisphosphate and cleaves the 6C intermediate into 2 3-phosphoglycerate. Stage 1 of the Calvin Cycle - CORRECT ANSWER >>>>3 ribulose 1-5-bisphosphate + 3 CO2 --> 6 3-phosphoglycerate. Catalyzed by rubisco 65 | P a g e Glycolate Cycle - CORRECT ANSWER >>>>Process of converting 2-phosphoglycerate to 3-phosphoglycerate in chloroplast, peroxisome, and mitochondria. C4 Plants - CORRECT ANSWER >>>>Fix CO2 into PEP to form oxaloacetate (via PEP carboxykinase) that is then converted to malate that carries CO2 to rubisco. Bypasses O2 binding. CAM plants - CORRECT ANSWER >>>>Fix CO2 into PEP to form oxaloacetate (via PEP carboxykinase) that is converted to malate at night and stored until the day time. Malonyl-CoA - CORRECT ANSWER >>>>Formed from Acetyl-CoA and HCO3 via the Acetyl-CoA carboxylase (ACC). Serves as a regulator of FA catabolism and precursor in FA synthesis. 66 | P a g e ACC (acetyl-CoA carboxylase) Regulation - CORRECT ANSWER >>>>Inhibited by PKA in glucagon chain and activated by pjhosphatase in INSR chain. FAS (Fatty-acid Synthetase) - CORRECT ANSWER >>>>Catalyzes condensation, reduction, dehydration, and reduction of growing fatty acid chain. Requires activation by acetyl-CoA or malonyl-CoA Additional Cost of FAS in Eukaryotes - CORRECT ANSWER >>>>Acetyl-CoA for lipid synthesis is made in mitochondria and must be transferred into the cytosol via citrate transporter. Costs 2 ATP. Cost of FAS in Eukaryotes - CORRECT ANSWER >>>>3 ATP's per 2 carbon unit added. Phosphatidic Acid - CORRECT ANSWER >>>>Common precursor to TAGs and 67 | P a g e phospholipids. Consists of a glycerol 3- phosphate with two acyl groups that are attached via acyl transferases. TAGs (Triacylglycerols) - CORRECT ANSWER >>>>Made from phosphatidic acid by removing phosphate with phosphatase and adding an acyl group with acyl transferase. Cholesterol Synthesis - CORRECT ANSWER >>>>Synthesized from 15 acetyl-CoA through a number of intermediates. HMG-CoA Reductase - CORRECT ANSWER >>>>Enzyme that converts ß-hydroxy-ß-methyl glutaryl-CoA to mevalonate in cholesterol metabolism. Regulation of HMG-CoA Reductase - CORRECT ANSWER >>>>Inhibited by AMPK (AMP dependent kinase), glucagon, and oxysterol. Activated by insulin.