Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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A sample of glycogen from a patient with liver disease is incubated with Pi, normal glycogen phosphorylase, and normal debranching enzyme. The ratio of glucose 1-phophate to glucose in the reaction mixture is 100. What is the patient’s most likely enzymatic deficiency?
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- Degradation of normal glycogen results to 97.2% glucose 1-phosphate and 7.2% glucose. Assuming a ratio of glucose 1-phosphate to glucose recorded in a glycogen sample from a patient with a liver disease was 100, The patient’s most likely enzymatic deficiency is _________arrow_forwardOutline the mechanism of the conversion of a-ketoglutarate to succinylCoA catalyzed by α-ketoglutarate dehydrogenase complex. Include all products, coenzymes, and reactions in your discussion.arrow_forwardIntestinal microbes produce butyrate, which helps regulate the immune system. How many rounds of β oxidation of palmitate are required to produce butyrate?arrow_forward
- What glycolytic intermediate is fructose converted to in the liver, such that it can be utilized in glycolysis? Glyceraldehyde 3-phosphate Glucose 6-phosphate Fructose 6-phosphate Fructose 1-phosphatearrow_forwardGierke disease (glycogenosis) arises in the inherited defect of glucose-6-phosphatase and is accompanied by swelling of liver and hypoglycemia inpostabsorptive period. Why does a fasting blood glucose level of patients fallsharply in the morning? To answer this question:a) draw the scheme of the mobilization of the main reserve homopolysaccharideinvolving glucose-6-phosphatase in a healthy person and indicate the localizationof this process in the organism;b) explain the role of this metabolic pathway.arrow_forwardInterestingly, the most common treatment for methanol poisoning is to use ethanol as an antidote. Why would adding large amounts of ethanol help slow down the rate of formic acid production by aldehyde dehydrogenase?arrow_forward
- Indicate what will happen (increase, decrease or no effect) to the activity of the enzyme or rate of the metabolic pathway given the following conditions.arrow_forwardSelect the single best answer. What reaction does the enzyme triose phosphate isomerase catalyze? Conversion of dihydroxyacetone phosphate into glyceraldehyde-3-phosphate. Isomerization of 3-phosphoglycerate into 2-phosphoglycerate. Substrate level phosphorylation involving transfer of a phosphoryl group from 1,3-bisphosphoglycerate into 3-phosphoglycerate. Isomerization of glucose-6-phosphate into fructose-6-phosphate.arrow_forwardFor each of the following situations, predict the major concequences for glycogen metabolism. Explain your logic in a few sentences. Will the amount of glycogen be higher or lower than the normal or unchanged. a) Effect of mutation Y194F in glycogenenin on glycogen synthesis. b) Effect on the loss of the gene that encodes inhibitor I of protein phosphatase I on both glycogen phosphorylase and glycogen synthase. c) Effect on the substrate analog shown below in glycogen synthesis (hint: what is the normal reaction sequence? At which step in the pathway does this sequence become blocked and why?)arrow_forward
- Suggest a name for an enzymes that catalyzes each of the following reactions.1. Hydrolysis of Lactose 2. Oxidation of Nitrate3. Decarboxylation of Citrate4. Reduction of Exalatearrow_forwardWhat if the phosphate group for the glycolysis reaction with enzyme glyceraldehyde 3-phosphate dehydrogenase was from ATP instead of Pi? What would the complete, balanced, net rxn of glycoslysisequation be and how does this impact the overall glycolysis rxn?arrow_forwardFor the two conditions below regarding Glycogenolysis, please explain how glucose release would be affected. Would there be an increased, decrease, or no change compared to “normal” conditions? Also explain which enzyme or reaction is affected and why. Condition 1: the debranching enzyme is inhibited Condition 2: free inorganic phosphate is chelatedarrow_forward
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