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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Chapter 21, Problem 15P
Interpretation Introduction
Interpretation:
Different signs of the absence of glycogen phosphorylase shown by Hers and McArdle diseases and the genetic nature of the phosphorylase should be stated.
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What is the effect of a defective a(1→ 4) phosphatase in Pompe's disease (GSD II)?
O Accumulation of abnormal, unbranched glycogen, leading to heart or liver failure and short fife expectancy
O Glycogen accumulation in heart, leading to heart failure, muscle weakness, short life expectancy
O Absence of UDP-glucose conversion to glycogen, leading to lack of muscle glycogen, exercise intolerance
Glycogen accumulation due to lack of glucose-6-phosphate conversion to glucose, leading to liver enlargement,
hypoglycemia, short life expectancy
O Lack of complete degradation of glycogen to glucose. leading to mild hypoglycemia, enlarged liver and muscle weakness
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Different control mechanisms are used to regulate the synthesis of glycogen. Match the action on the left with the effect
on the right.
Increase in the
concentration of
inorganic phosphate ion
Decrease in the activity of
phosphoprotein
phosphatase
Phosphorylation of
glycogen phosphorylase
Dephosphorylation of
glycogen synthase
Ű
Clear All
Decreasing glycogen
synthesis
Increasing glycogen
synthesis
No effect on glycogen
synthesis
Protein Phosphatase 1:
What overall effect does PP1 have on the storage or breakdown of glycogen? (1 point)
How does PPI regulate the activity of its targets? (1 point)
Which enzymes are its targets? (2 points)
What activates it [hormone (pathway activator) and enzyme (immediate activator)]? (2 points)
Hormone:
Enzyme:
Chapter 21 Solutions
Biochemistry
Ch. 21 - Prob. 1PCh. 21 - Prob. 2PCh. 21 - Prob. 3PCh. 21 - Prob. 4PCh. 21 - Prob. 5PCh. 21 - Prob. 6PCh. 21 - Prob. 7PCh. 21 - Prob. 8PCh. 21 - Prob. 9PCh. 21 - Prob. 10P
Ch. 21 - Prob. 11PCh. 21 - Prob. 12PCh. 21 - Prob. 13PCh. 21 - Prob. 14PCh. 21 - Prob. 15PCh. 21 - Prob. 16PCh. 21 - Prob. 17PCh. 21 - Prob. 18PCh. 21 - Prob. 19PCh. 21 - Prob. 20PCh. 21 - Prob. 21PCh. 21 - Prob. 22PCh. 21 - Prob. 23PCh. 21 - Prob. 24PCh. 21 - Prob. 25PCh. 21 - Prob. 26PCh. 21 - Prob. 27PCh. 21 - Prob. 28PCh. 21 - Prob. 29PCh. 21 - Prob. 30PCh. 21 - Prob. 31PCh. 21 - Prob. 32PCh. 21 - Prob. 33PCh. 21 - Prob. 34PCh. 21 - Prob. 35PCh. 21 - Prob. 36PCh. 21 - Prob. 37PCh. 21 - Prob. 38PCh. 21 - Prob. 39PCh. 21 - Prob. 40PCh. 21 - Prob. 41PCh. 21 - Prob. 42PCh. 21 - Prob. 43PCh. 21 - Prob. 44PCh. 21 - Prob. 45PCh. 21 - Prob. 46P
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- In the following diagram of glycolysis. Identify the steps that are amphibolic, taking place in both glycolysis and gluconeogenesis. Also, identify the regulated steps and what compounds act as regulators.arrow_forwardLactic acid builds up in the athlete's thigh muscle after marathon training. Compare and contrast the physiological functions and Vmax of glycogen phosphorylase in active skeletal muscle and liver. The athlete faints after a rigorous workout owing to a low blood glucose level. A liver biopsy reveals that there is an excess of glycogen in the liver. Suggestions on whatever sort of enzyme is faulty in this circumstance should be accompanied by an explanation.arrow_forwardHers disease results from an absence of liver glycogen phosphorylase and may result in serious illness. In McArdle disease, muscle glycogen phosphorylase is absent. Although exercise is difficult for patients suffering from McArdle disease, the disease is rarely life threatening. Account for the different manifestations of the absence of glycogen phosphorylase in the two tissues. What does the existence of these two different diseases indicate about the genetic nature of the phosphorylase?arrow_forward
- Describe the impact of phosphorylation of glycogen phosphorylase on its heterotropic regulation. (Don’t need the structural details; focus on the qualitative effects on allostery; be brief and to the point)arrow_forward. Glucagon secretion causes inhibition of intracellular acetyl-CoA car- boxylase activity by several mechanisms. Name all you can think of.arrow_forwardWhy would LDH be up- or down-regulated depending on location of cancer cells? Anaerobic cancer cells enhance rates of ATP production and rely on pyruvate to lactate conversion. LDH5 expressed can vary in favoring pyruvate for conversion to lactate (anaerobic metabolism). Aerobic compartments in newly formed fibrobasts and vessels use lactate to convert to pyruvate for oxidative phosphorylation and favor lactate conversion to pyruvate by LDH1 (aerobic metabolism). Lactate dehydrogenase is upregulated in both cancer cells and supporting stroma and vessels, thus only LDH5 is upregulated showing enhanced expression levels and thus presence at the plasma membrane to increase levels of lactate for export, LDH1 levels are always consistent. LDH1 is upregulated in response to the export of lactate by MCT1, while LDH5 is down-regulated Neither LDH1 or LDH5 are both consistently expressed, regardless of oxygen levelsarrow_forward
- During ketosis brought on by a ketogenic diet, liver gluconeogenesis rates are high True Falsearrow_forwardPlease select appropriate word in each bracket Glycogen provides short term energy storage primarily in liver and muscle. Defects in the enzymes that are required for either glycogen synthesis or breakdown therefore affect levels of [ Select ] ["glucose", "glycogen"] in the bloodstream and the amount of glycogen in the liver. This is exemplified by defects in [ Select ] ["glucose-6-phosphatase", "glycogen synthase"] , which is a deficit in breakdown and delivery, whereas mutations compromising [ Select ] ["glycogen synthase", "glycogen debranching enzyme"] result in a defect in synthesis, but defects in either enzyme produce [ Select ] ["hypoglycemia", "hypothermia"].arrow_forwardNumber the oxygens(1-6) in any order. Trace the path of this glucose through pathways of glycolysis and the TCA cycle and determine which step of the pathways each oxygen is removed from the process.arrow_forward
- It is absolutely not necessary to produce amylase in an active form in our body. But it is not in the case of trypsin. Given reasons.arrow_forwardDeficiencies of carnitine, carnitine acyltransferases, or carnitine/acylcarnitine translocase affect the metabolism of long-chain fatty acids. Many of the symptoms are similar, and include hypoketotic hypoglycemia, low ketone levels and low blood sugar with fasting, and damage to the liver, heart, or muscles due to fatty acid buildup in those tissues. Symptom severity varies with the form of the deficiency. The following abbreviations are used: carnitine acyltransferase (carnitine palmitoyltransferase), CPT and carnitine/acylcarnitine translocase, CACT. Identify each symptom or effect as a deficiency of CPT I, CPT II, or CACT. CPT I deficiency CPT II deficiency CACT deficiency Answer Bank acyl carnitine not transported into mitochondrial matrix long-chain fatty acids not transferred to carnitine long-chain fatty acids remain attached to carnitine in matrixarrow_forwardWhen glycogen is degraded (catabolized), all of the following occur in both liver and muscle EXCEPT Active glycogen phosphorylase catalyzes the phosphorolysis of alpha-1,4- glucosidic bonds in glycogen. The conversion of glycogen phosphorylase a to glycogen phosphorylase b is a major control step. Glucose-1-phosphate is converted to glucose-6-phosphate by phosphoglucomutase. High concentrations of glucose and AMP act as important control factors. Debranching enzyme catalyzes the hydrolysis of alpha-1,6-glucosidic bonds in glycogen.arrow_forward
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