Step 2: Acyl-AMP +→ acyl-CoA +COACOA + ADPPP i2 ADPCoAThe acyl-CoA synthetly reversible, withAMPm constant near 1.to favor formation of fATPATP The enzyme-bound intermediate in this reaction has been identified as the mixed anhydride of the fatty acid and adenosine2ºmonophosphate (AMP), acyl-AMP.R-C-O-P-O-CH20-Adenine0.HHHHOHOHComplete the two equations corresponding to the two steps of the reaction catalyzed by acyl-CoA synthetase.Step 1: R-COO¯+→ acyl-AMP +COAATPStep 2: Acyl-AMP +AMP→ acyl-ADP + PH₂OH+ATPCOAThe acyl-CoA synthePPn is readily reversibiPP;ibrium constant near 1. How can this reaction be made1

Answered: Image /qna-images/answer/502a3d2e-ef3c-4bb4-b2b1-d7efc08c2370.jpg

Answered: Step 2: Acyl-AMP + → acyl-CoA + COA COA…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 16P: Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for...

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Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.
Fatty acids are converted to their coenzyme A esters in a reversible reaction catalyzed by acyl-CoA synthetase: R-COO +ATP +COA R-C-COA +AMP + PPi a) The reaction involves two steps the first of which forms an enzyme-bound intermediate identified as the mixed anhydride of the fatty acid and AMP: R-C-O-P-O-nibose-adenine Write two chemical equations coresponding to the two steps of the reaction catalyzed by the synthetase. b) The acyl-CoA synthetase reaction as written above is readily reversible. How might the reaction be made to favor formation of fatty acyl-CoA? Write within the box. Anything outside the box will not be graded. From the
Incubation of the norsolinic acid synthase holo-ACP with malonyl CoA gave malonyl-S-ACP (molecular weight 10112 Da). (ACP SH holo-ACP Malonyl-SNAC Calculate the molecular weight of holo-ACP. (ACP OH malonyl-S-ACP MW = 10112
In humans, the biosynthesis of L-glutamine is catalyzed by the L-glutamine synthetase. The global reaction can be written as follows: ATP + glutamate + NH3 ADP + phosphate + glutamine The A,Gº' value for this reaction is -16.3 kJ.mol-1 (from left to right). 1- Explain the significance this information. 2- This reaction can be considered as the sum of two component reactions which are exergonic and endergonic, respectively, under standard conditions. Write these two component reactions and evaluate A,Gº of the endergonic reaction. Data: A,Gº of ATP hydrolysis = -30.4 kJ mol-¹
In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.
The enzyme Glucose-6-phosphate dehydrogenase catalyzes the nicotinamide adenine dinucleotide oxidation of cyclic glucose-6-phosphate to form the lactone product shown below. Propose a mechanism for this reaction showing all electron flow (using the arrow convention). You must draw the substrate glucose-6-phosphate (the configuration of the anomeric carbon does not matter) and the “business end” of the cofactor.
Draw the structures of the following coenzyme molecules: 1. CoA-SH/Acetyl-S-CoA 2. NAD*/NADH + H* • For both: Give full name (if you copy the formula from an Internet source, please cite it properly, for example, according to the Chicago Manual of Style. • Indicate what are the chemical groups that are active in these molecules, i.e., what group participates in metabolic reactions (be aware that both molecules may be involved in both anabolic and catabolic processes). • What vitamin or vitamins will, when modified, contribute to the structure of these molecules? • Write a short, general conclusion of the importance of these two coenzymes in metabolism.
Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
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?
One of the regulators of the TCA cycle is succinyl CoA. Discuss the rationale for this molecule to be used to regulate the TCA cycle [include chemical structures and chemical equations where appropriate]. What is an allosteric inhibitor? How does it operate? For what TCA enzymes does succinyl CoA act as an inhibitor? What is the metabolic role of succinyl CoA? So then why is this molecule a reasonable choice as an inhibitor of the TCA?
In the hydrolysis of ATP to ADP and Pi, the equilibrium concentration of ATP is too small to be measured accurately. A better way of determining K’eq, and hence ΔG◦’ of this reaction, is to break it up into two steps whose values of ΔG◦’ can be accurately determined. This has been done using the following pair of reactions (the first being catalyzed by glutamine synthetase): (1) ATP + glutamate + NH3 ⇌ ADP + Pi + glutamine + H+ ΔG1◦’= -16.3 kJ/mol (2) glutamate + NH3 ⇌ glutamine + H2O + H+ ΔG2◦’= 14.2 kJ/mol What is the ΔG◦’ of ATP hydrolysis according to these data and is the overall reaction spontaneous? What is the value of the equilibrium constant for the overall reaction at 25.0 °C. If the concentration of ATP at equilibrium is 20.0 mM and the concentration of ADP at equilibrium is 50 nM. What is the concentration the phosphate group (in mM) at equilibrium?
Some bacteria use the citric acid cycle intermediate, a-ketoglutarate, plus acetyl-CoA, as the starting point for lysine biosynthesis. The first part of this biosynthetic pathway uses the same chemical strategy found in the citric acid cycle. Propose a four-step pathway for the conversion of a-ketoglutarate to 2-oxoadipate. Draw the three missing intermediates, and indicate the chemistry involved in each reaction. Include any cofactors that you think might be required for specific steps.

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