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Consider the following ... carbohydrates and glycolysis BIOCHEMIS • Glycolysis: An interesting mechanism / Triose Phosphate Isomerase (TIM) "catalytic perfection" diffusion rate limited S.cerevisae (2019 FEBS Journal) / kcat/Km = 1.14 x 10° M1's" / kcat = 6.40 x 10'sª / Km = 1.4 x 10³M

Consider the following ... carbohydrates and glycolysis BIOCHEMIS • Glycolysis: An interesting mechanism / Triose Phosphate Isomerase (TIM) "catalytic perfection" diffusion rate limited S.cerevisae (2019 FEBS Journal) / kcat/Km = 1.14 x 10° M1's" / kcat = 6.40 x 10'sª / Km = 1.4 x 10³M

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Complete this mechanism
**Consider the following … carbohydrates and glycolysis** **Glycolysis: An interesting mechanism / Triose Phosphate Isomerase (TIM)** **“Catalytic perfection” diffusion rate limited** *S. cerevisiae* (2019 FEBS Journal) k_cat/K_m = 1.14 x 10^8 M^-1s^-1 / k_cat = 6.40 x 10^3 s^-1 / K_m = 1.4 x 10^-3 M **Mechanism Steps:** 1. **Substrate binds. Glutamate deprotonates carbon, resulting in enediol formation.** - The diagram shows a chemical reaction where an oxygen atom bound to a glutamate residue deprotonates a carbon, forming an enediol structure. Arrows indicate the movement of electrons during this process. 2. **Enzyme changes conformation. Histidine deprotonates primary alcohol.** - This step illustrates the interaction where the structure's conformation allows histidine to remove a proton from the primary alcohol group, depicted with arrows showing electron shifts. 3. **Electrons flow back through a double bond into aspartate to generate aldehyde product.** - The final step highlights the flow of electrons back into a double bond, which transforms into aspartate, resulting in the formation of an aldehyde product, as indicated by electron movement arrows. **Notes:** *(Additional notes can be included here as needed for further understanding.)*
Transcribed Image Text:**Consider the following … carbohydrates and glycolysis** **Glycolysis: An interesting mechanism / Triose Phosphate Isomerase (TIM)** **“Catalytic perfection” diffusion rate limited** *S. cerevisiae* (2019 FEBS Journal) k_cat/K_m = 1.14 x 10^8 M^-1s^-1 / k_cat = 6.40 x 10^3 s^-1 / K_m = 1.4 x 10^-3 M **Mechanism Steps:** 1. **Substrate binds. Glutamate deprotonates carbon, resulting in enediol formation.** - The diagram shows a chemical reaction where an oxygen atom bound to a glutamate residue deprotonates a carbon, forming an enediol structure. Arrows indicate the movement of electrons during this process. 2. **Enzyme changes conformation. Histidine deprotonates primary alcohol.** - This step illustrates the interaction where the structure's conformation allows histidine to remove a proton from the primary alcohol group, depicted with arrows showing electron shifts. 3. **Electrons flow back through a double bond into aspartate to generate aldehyde product.** - The final step highlights the flow of electrons back into a double bond, which transforms into aspartate, resulting in the formation of an aldehyde product, as indicated by electron movement arrows. **Notes:** *(Additional notes can be included here as needed for further understanding.)*
Expert Solution
Step 1

Triosephosphate isomerase is the isomerase enzyme which involves in the isomerization reaction in the preparative phase of glycolytic metabolism.Where aldose ketose sugar was converted to ketose sugar - dihydroxyacetophosphate was converted to glyceraldehyde-3-phosphate.

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