Propose a detailed chemical mechanism for the enzyme catalyzed reaction below andbriefly note similarities, if any, to enzymes that we've studied.CO2+ CO22CO2HOCH3

Step 1:Proposed Chemical MechanismActivation of Bicarbonate (CO2 Source)The enzyme binds…

Answered: Propose a detailed chemical mechanism…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter20: Electron Transport And Oxidative Phosphorylation

Section: Chapter Questions

Problem 19P

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Similar questions

PREDICT In the following reaction series, which enzyme(s) is/are most likely to have an allosteric site to which the end product E binds? (a) enzyme 1 (b) enzyme 2 (c) enzyme 3 (d) enzyme 4 (e) enzymes 3 and 4
Figure 6.8 Look at each of the processes shown, and decide if it is endergonic or exergonic. In each case, does enthalpy increase or decrease, and does entropy increase or decrease?
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
Which of the following comparisons or contrasts between endergonic and exergonic reactions is false? Endergonic reactions have a positive ?G and exergonic reactions have a negative ?G Endergonic reactions consume energy and exergonic reactions release energy Both endergonic and exergonic reactions require a small amount of energy to overcome an activation barrier Endergonic reactions take place slowly and exergonic reactions take place quickly.
Both prokaryotic and eukaryotic organisms carry out some form of glycolysis. How does ha fact support or not support the assertion that glycolysis is one of the oldest metabolic pathways?
Based on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.
Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?
In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
How Art the Enzymes of Metabolic Pathways Organized? Name the four principal modes of enzyme organization in metabolic pathways.

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Propose a detailed chemical mechanism for the enzyme catalyzed reaction below and briefly note similarities, if any, to enzymes that we've studied. CO2 + CO2 2 CO2 HO CH3