Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 22, Problem 22P
Interpretation Introduction
Interpretation:
Role of Arg-22 in the conformational state change between the R and T state.
Introduction:
Fructose-1,6-bisphosphatase enzyme is involved in the fructose-1,6-bisphosphate to fructose 6-phosphate conversion that takes place in the gluconeogenesis and the Calvin cycle.
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Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. The mammalian enzyme is tetrameric, negatively regulated by both Fructose 2,6-bisphosphate and AMP. Propose three (3) distinct models for how these molecules regulate FBPase activity. Also, describe how the enzyme might differentiate between Fructose 1,6 bisphosphate and Fructose 2,6-bisphosphate binding to the allosteric site on the enzyme with particular emphasis on amino acids comprising the allosteric binding site(s).
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Chapter 22 Solutions
Biochemistry
Ch. 22 - Prob. 1PCh. 22 - Prob. 2PCh. 22 - Prob. 3PCh. 22 - Prob. 4PCh. 22 - Prob. 5PCh. 22 - Prob. 6PCh. 22 - Prob. 7PCh. 22 - Prob. 8PCh. 22 - Prob. 9PCh. 22 - Understanding Enzyme Mechanisms Related to...
Ch. 22 - Understanding the Mechanisms of Reactions Related...Ch. 22 - Prob. 12PCh. 22 - Prob. 13PCh. 22 - Prob. 14PCh. 22 - Prob. 15PCh. 22 - Prob. 16PCh. 22 - Prob. 17PCh. 22 - Prob. 18PCh. 22 - Prob. 19PCh. 22 - Prob. 20PCh. 22 - Prob. 21PCh. 22 - Prob. 22PCh. 22 - Using the ActiveModel for aldose reductase,...
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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.arrow_forwardConsider the role of Histidine in the Serine protease mechanism and sketch a plot showing the predicted pH profile of chymotrypsin which has a pH optimum of approximately ~8. The pk, for the His in the catalytic triad is 7.3 in free chymotrypsin which increases to greater than 8 with a bound peptide. Be sure to label the plot axes and indicate the pka of His on the plot,arrow_forwardDescribe two types of regulation of the enzyme glutamine synthetase and explain why the regulation of this enzyme is soooo complex.arrow_forward
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- The enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATEarrow_forwardFrom the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?arrow_forwardDiagram the hydrogen-bonding interactions of the catalytic triad His–Lys–Ser during catalysis in a hypothetical hydrolytic enzyme.arrow_forward
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