Hexokinase catalyzes phosphorylation of glucose to clucose-6-phosphate, where ATP is used as a donor of phosphate group, this i an example of: Select one: O O a. Oxidoreductase b. Ligase c. Lyase d. Transferase
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- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.X INCORRECT; see section 13.1 Enzymes occasionally display weak "“side" activities. Draw the structure of the product (other than ADP) of the reaction that results when pyruvate kinase, operating in reverse, uses lactate as a substrate. For your structure: 1. Do not include primary or secondary hydrogens. CH2 HO OH Edit DrawingG. ENZYME CLASSIFICATION. Identify the main class of enzymes used to catalyzed the following reactions: 1. Lactate dehydrogenase: NADH+H NAD HC-OH CH3 CH Pynnte Lactate 2. Methylmalonyl-CoA mutase: CH CH SCOA CH,CH, SCOA coenzyme B12 COO COO methylmalonyl-CoA succinyl-CoA 3. Enolase: 0. H–Ċ–0–P–0- C-0–P-0- + H,0 HO–CH, CH 6 Phosphoenolpyruvate 2-Phosphoglycerate 4. Chymotrypsin: -0–CH,CH3 + H2O - RCOOH + HOCH,CH3 5. Pyruvate carboxylase: coo • co, • ATP + H,0 H-C-H . ADP + P, + 2H čoo CH, Pyruvate Oxaleacetate
- Compare and contrast biochemical pathways. Describe the chemistry of the last three steps of the TCA. Describe the chemistry of the first three steps of β-oxidation. Explain how these pathways are similar and how they differ in terms of their chemistry, the involvement of coenzymes and the fate of the electrons. Describe the two connections between the urea cycle and the citric acid cycleExplain biochemical pathways mechanistically. Describe the β-oxidation pathway. Describe the conversion of propionyl CoA to succinyl CoA. Describe the substrate activation processes in the urea cycle (CPS 1 and arginosuccinate synthetase).Decide whether each of the following statements is true about leucine transaminase. It's an enzyme, and leucine is its substrate. It speeds up the rate at which leucine is converted to other substances. It's a small molecule, with a molecular weight around 50 mol If you were to write a chemical equation for certain biochemical reactions of leucine, leucine transaminase would appear on both sides. Otrue Ofalse Otrue Ofalse Otrue Ofalse Otrue Ofalse X
- 1) Tabulate the differences and/ or similarities of the different kinds of coenzymes and cofactors. Structure Source ATP SAM COA Retinal THF- tetrahydrofolate Vitamin K NAD, NADP FMN, FAD TPP PLP Adenosylcobalamin methylcobalamin and Function/ Role/ ImportanceIn class, I mentioned that fructose is metabolized differently in the liver compared to glucose. Refer to the figure shown below to calculate the number ofATPs you would expect from the metabolism of fructose in the liver. Show your work! Fructokinase Fructose Fructose-1-P АТР ADP Aldolase B Dihydroxy- acetone phosphate Glyceraldehyde АТР Triose kinase Triose phosphate isomerase ADP 4 - Glyceraldehyde-3-P Glycolysis Руruvate Acetyl-CoA Fatty acids and triglyceridesDraw Gluconeogenesis. Please make sure to state all the enzymes and co-factors for each step of the pathway. note you are responsible for all the enzymes for each step, even though it is not stated on the slide.
- 5. You discover a new cysteine protease similar to papain. Cysteine proteases are proteolytic enzymes that utilize a cysteine residue in the active site for the nucleophilic attack of a peptide bond, while a second residue acts as a base for proton abstraction in the reaction (acid base catalysis). In this novel enzyme the pKa of the cysteine residue is significantly lowered by the active site environment to pKa=4. a. Knowing that the protease shows highest activity between pH 4-6, what could be the identity of the base residue acting as a in the reaction? Explain and write the expected mechanism for the reaction. SH он. Because of the position of arsenic in the periodic table, arsenate (AsO}-) is chemically similar to inorganic phosphate and is used by phosphate-requiring enzymes as an alternative substrate. However, organic arsenates are quite unstable and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.Part A Identify each of the following metabolic pathways. Drag the appropriate labels to their respective targets. Reset Help the conversion of fatty acids to 2-carbon units of acetyl CoA ketogenesis the conversion of an amino acid to an a-keto transamination acid the combination of 2-carbon units of acetyl COA to form fatty acids oxidative deamination the removal of an amino group as NH4+ from B oxidation glutamate to yield a-ketoglutarate lipogenesis the production of ketone bodies