Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 26, Problem 11P
The Catabolism of Uric Acid Write a balanced equation for the oxidation of uric acid to glyoxylic acid,
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There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.
What are the equilibrium concentrations of fructose 1,6-bisphosphate, dihydroxyacetone phosphate, and glyceraldehyde 3-phosphate when 1 mM fructose 1,6-bisphosphate is incubated with aldolase under standard conditions?
NOTE: the enzyme-inhibitor complex requires 450 joule/mol to dissociateJOULE/MOL
Chapter 26 Solutions
Biochemistry
Ch. 26 - Prob. 1PCh. 26 - Prob. 2PCh. 26 - Allosteric Regulation of Purine and Pyrimidine...Ch. 26 - Inhibition of Purine and Pyrimidine Metabolism by...Ch. 26 - Prob. 5PCh. 26 - Allosteric Regulation of Ribonucleotide Reductase...Ch. 26 - Prob. 7PCh. 26 - Prob. 8PCh. 26 - Prob. 9PCh. 26 - Prob. 10P
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- Diagram the reactions involving glutamate dehydrogenaseand glutamine synthetase that produce glutamine from ammoniaand -ketoglutarate.arrow_forwardDescribe the two phases of the the HMP shunt. Enumerate the reactions in each phase and the corresponding enzyme of each reation. Explain how the HMP shunt is regulated?arrow_forwardEthylene glycol (HO−CH2−CH2−OH) is a major component of antifreeze. In the body, it is first converted to HOOC−CHO (oxoethanoic acid) and then to HOOC−COOH (oxalic acid), which is toxic. What class of enzyme catalyzes both of the reactions of ethylene glycol? The treatment for the ingestion of ethylene glycol is an intravenous solution of ethanol. How might this help prevent toxic levels of oxalic acid in the body?arrow_forward
- Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)arrow_forwardName: Date: Year/Section: Score: ACTIVITY 5.1.1 Determine the catalytic power of jack bean urease in catalyzing the hydrolysis of urea given the following conditions: At 20C, the rate constant for enzyme-catalyzed reaction is 3x104/sec The rate constant for the uncatalyzed hydrolysis of urea is 3x10-10/sec. ACTIVITY 5.1.2 Give examples of enzymatic reaction for each type of specificity 96 Copyright 2019. All Rights Reserved. 2--------arrow_forwardNormal carbonic anhydrase has zinc at its active site . Suggest a structural reason why carbonicanhydrase synthesized with Ni²⁺, Fe²⁺, or Mn²⁺ in place of Zn²⁺ gives an enzyme with less catalytic efficiency.arrow_forward
- In less than 100 words total i) describe the physiological reaction of the red population to alcohol consumption, which is usually not seen with the blue population, and ii) explain in the language of this unit how the enzymatic properties of aldehyde dehydrogenase relate to this physiological reaction.arrow_forwardOutline the path of 2 molecules of alanine to 1 molecule of glucose using alanine dehydrogenase and other processes or pathways you know. Determine the net reaction and make sure you include both the necessary cofactors AND the handling of the ammonia by the urea cycle.arrow_forwardConsider the enzyme pancreatic amylase, which has an optimum pH of 7.0. How is the rate of a pancreatic amylase-catalyzed reaction affected by each of the following changes: (a) lowering the pH from 7 to 4; (b) increasing the pH from 7 to 9; (c) decreasing the temperature from 37 °C to 28 °C; (d) increasing the temperature from 37 °C to 50 °C?arrow_forward
- The glucose oxidase (GOD) method is commonly used to determine blood glucose level. Explain, the principle of GOD method by regarding reactions.arrow_forwardXanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess uses gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student searcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO hich uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the neweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table Table 1. Enzyme Kinetic Data Velocity, mM/s Kmp 0.0351 [S], mM Cha Хan 0.492 0.0678 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Enzyme Kinetic Parameter: Parameters Vmax |Ku | Type of Inhibition Mode of Binding Xanthine Kaempferol Chlorogenic acid NA NA Line Weaver Burk Plot:arrow_forwardAldolase is a key enzyme in glycolysis that catalyzes the cleavage of its substrate, fructose-1,6-bisphosphate, into glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. The lysine and tyrosine shown are enzyme residues essential in the presented mechanism. Pi indicates inorganic phosphate. a. Which residue, if any, is acting as a general acid in the mechanism shown above? Explain your choice. b Which of the following type(s) of catalysis is/are involved in the mechanism above? Covalent catalysis Metal ion catalysis General acid/base catalysis none of the above c. Scientists prepared a mutant of aldolase in which tyrosine was replaced with serine. They found that the KM value for fructose-1,6-bisphosphate remained the same in the mutant as the original wild type (WT) enzyme. The value of kcat, however, decreased by a factor of 1000. Would Vmax be altered for the mutant enzyme? If so, by how much? Explain your answer. Would deltaG of the reaction be altered for the…arrow_forward
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