Lysine catabolism begins with reductive amination of a-ketoglutarate to give saccharopine in a multistep process.Draw curved arrows to show the movement of electrons in this step of the reaction mechanism.Arrow-pushing Instructions7COOH NH3COOOOCB:COOH NH3COOBH+

Answered: Lysine catabolism begins with reductive…

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter29: The Organic Chemistry Of Metabolic Pathways

Section29.SE: Something Extra

Problem 23MP: One of the steps in the pentose phosphate pathway for glucose catabolism is the reaction of...

See similar textbooks

Similar questions

One of the steps in the pentose phosphate pathway for glucose catabolism is the reaction of xylulose 5-phosphate with ribose 5-phosphate in the presence of a transketolase to give glyceraldehyde 3-phosphate and sedoheptulose 7-phosphate. (a) The first part of the reaction is nucleophilic addition of thiamin diphosphate (TPP) ylide to xylulose 5-phosphate, followed by a retro-aldol cleavage to give glyceraldehyde 3-phosphate and a TPPcontaining enamine. Show the structure of the enamine and the mechanism by which it is formed. (b) The second part of the reaction is addition of the enamine to ribose 5-phosphate followed by loss of TPP ylide to give sedoheptulose 7-phosphate. Show the mechanism.
Acetolactate synthase transfers the acyl group of pyruvate to alpha-ketobutyrate. This is the first step in the biosynthesis of the amino acid isoleucine. Propose a mechanism for this reaction.
Imidazoleglycerol‑phosphate dehydratase is an enzyme in the histine biosynthesis pathway. It catalyzes the E1 dehydration of D‑erthyro‑imidazole‑glycerol phosphate to imidazole acetol‑phosphate. This is a rare example of a biological E1 reaction, as most biological elimination reactions occur through E1cB instead. In this reaction, D‑erthyro‑imidazole‑glycerol phosphate is first protonated to form a good leaving group. Then, the leaving group is ejected to form the resonance‑stabilized carbocation shown. Draw curved arrows forming the most stable resonance structure to explain why this reaction goes through an E1 mechanism. Draw curved arrows to form the most stable resonance structure.
Neostigmine is an inhibitor of acetylcholinesterase. The enzyme attempts to catalyse the same reaction on neostigmine as it does with acetylcholine. However, a stable intermediate is formed which prevents completion of the process and which results in a molecule being covalently linked to the active site. Identify (draw) the stable intermediate and explain why it is stable.
a Lactate dehydrogenase H H3C-C-coO- ОН ooc-C-CH3 L-(+)-Lactase Pyruvate This is a(an) b Creatine kinase CH3 O CH3 O H2N, АТР ADP NH2 NH2 Adenosine triphosphate Adenosine diphosphate Creatine Phosphocreatine This is a(an)
None
Pyruvate carboxylase is thought to activate CO2 by ATP, through formation of carboxyphosphate as an intermediate. Propose a mechanism for the formation of this intermediate.
Please draw by hand. Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme's catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a base and an acid catalyst, respectively. Propose a mechanism for the reaction. ОН 2-03Р0 ОН dihydroxyacetone phosphate triosephosphate isomerase 2-03РО. H glyceraldehyde-3-phosphate FYI Glu is glutamic acid and his is histadine
Acetolactate synthase is another TPP-requiring enzyme. It transfers the acyl group of pyruvate to another molecule of pyruvate, forming acetolactate. This is the first step in the biosynthesis of the amino acids valine and leucine. Propose a mechanism for this reaction.
Acetolactate synthase is another TPP-requiring enzyme. It transfers the acyl group of pyruvate to another molecule of pyruvate, forming acetolactate. This is the first step in the biosynthesis of the amino acids valine and leucine. Propose a mechanism for this reaction.
An enzymatic assay was performed using the enzyme phophofructokinase-1, which catalyses the committed step of the glycolysis pathway. What is the final concentration of the fructose 6-phosphate substrate in a test tube containing the following: 250 µL of 150pM fructose 6-phophate, 100 µL 20 mg.ml-1 phosphofructoskinase-1 and 150 µL 100mM buffer pH 7.5
The following reaction is catalyzed by a PLP-dependent enzyme. Propose a mechanism for this reaction. H₂N H OH H OH H₂N XX 5

SEE MORE QUESTIONS

Recommended textbooks for you

Organic Chemistry

Chemistry

ISBN:

9781305080485

Author:

John E. McMurry

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305580350

Author:

William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:

Cengage Learning

Introduction to General, Organic and Biochemistry

Chemistry

ISBN:

9781285869759

Author:

Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305080485

Author:

John E. McMurry

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305580350

Author:

William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:

Cengage Learning

Introduction to General, Organic and Biochemistry

Chemistry

ISBN:

9781285869759

Author:

Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS

Lysine catabolism begins with reductive amination of a-ketoglutarate to give saccharopine in a multistep process. Draw curved arrows to show the movement of electrons in this step of the reaction mechanism. Arrow-pushing Instructions 7 COO H NH3 COO OOC B: COO H NH3 COO BH+