H.OHcoco2ноH co,1-isopropylmalate2-isopropylmalateBiosynthesis of leucine involves conversion of 1-isopropyimalate to 2-isopropylmalate (see above). This proceeds in four steps under basicenzymic catalysis via an isolable compound produced in step 2. Write a detailed mechanism for this conversion. Then, draw the intermediatecompound) produced in step 2.• You do not have to consider stereochemistry.• Draw uninvolved carboxyl groups in the anionic state, and enolates as carbanions.When needed, abbreviate CoenzymeA-S- as CH3S- In your drawing.aale

2-isopropylmalate synthase is a enzyme which catalyzes below chemical reaction with three…

Answered: Biosynthesis of leucine involves…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 18P: Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in...

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Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
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.
The Reactions and Meehanisms of the Leloir Pathway Write the reactions that permit galactose to be utilized in glycolysis. Write a suitable mechanism, tor one of these reactions.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
The catalytic efficiency of many enzymes depends on pH. Chymotrypsin, which has a well-known catalytic mechanism, shows a maximum value of kcat/Km at pH 8.0. A) Draw a pH curve of chymotrypsin activity over the pH range of 5 to 10 and briefly explain the rationale within the context of catalysis for your depiction. In particular, note how kcat and Km may change over this pH range. B) Enzymes of the a-amylase family catalyze a reaction by forming a covalent intermediate analogous to chymotrypsin, but to a conserved aspartate residue. Illustrate a catalytic mechanism containing a tetrahedral intermediate for a glycogen debranching enzyme based upon its potential membership in the a-amylase family. (don’t need to draw a whole glycogen)
Behenate (C22H44O2) can be obtained by chain elongation from palmitate. How many ATP equivalents are produced in the degradation of behenate to eleven acetyl-CoA?
Enolase catalyzes the reversible reaction shown below. Draw the detailed mechanism for the reaction that occurs in gluconeogenesis, namely the reaction of phosphoenolpyruvate to form 2-phosphoglycerate (the reverse direction in the reaction below).
Galactose 1-phosphate: UDP-glucose uridyltransferase (GALT) is an enzyme important for the catabolism of galactose. Patients with GALT deficiency present within days of birth with feeding difficulty, fatigue, jaundice and liver problems, and failure to thrive. In addition, a buildup of galactose and its metabolites are present in the bloodstream. GALT catalyzes the following reaction in galactose catabolism. NOTE that GALT is reversible!! Classify this enzyme and explain why you classified it in this way.
In working skeletal muscle under anaerobic conditions, glyceraldehyde 3-phosphate is converted to pyruvate (the payoff phase of glycolysis), and the pyruvate is reduced to lactate. Write balanced biochemical equations for all the reactions in this process, with the standard free-energy change for eachreaction. Then write the overall or net equation for the payoff phase of glycolysis (with lactate as the end product), including the net standard free-energy change.
Draw a schematic illustration of the hydrolysis of N-acetylphenylalaninamide catalyzed byalpha-chymotrypsin in which you indicate the important catalytic residues in the active site and how thesubstrate undergoes transformation to products through two different tetrahedral intermediates.
The high phosphoryl transfer potential of 1,3-bisphosphoglycerate is explained by the resonance stability of the product, 3-phosphoglycerate. The same explanation applies to the reaction that generates resonance stabilized pyruvate from phosphoenolpyruvate. Show the resonance structures for both products, 3-phosphoglycerate and pyruvate, and state why the reactant in both reactions is not resonance stabilized.

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