Questions and Answers
What is the function of aldolase?
What is the first step of the enzymatic mechanism of aldolase?
Substrate fructose-1,6-bisphosphate binds to enzyme.
What happens in step 2 of the reaction mechanism?
Epsilon amino group of Lys attacks the carbonyl of the substrate, forming protonated Schiff base with loss of H2O.
What occurs during step 3 of aldolase action?
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What is formed in step 4 after the enamine intermediate is protonated?
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What happens in step 5 of the aldolase mechanism?
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Study Notes
Function of Aldolase
- Catalyzes reaction 4 in glycolysis
- Cleaves biphosphorylated hexose into two 2-phosphorylated trioses
Substrate Binding
- Fructose-1,6-bisphosphate is the substrate that binds to the aldolase enzyme
- This initiates the first step of the enzymatic mechanism
Formation of Schiff Base
- The epsilon amino group of lysine attacks the carbonyl of the substrate
- This leads to the formation of a protonated Schiff base and the loss of water
Aldol Cleavage
- Aspartate acts as a general base, facilitating aldol cleavage
- Cleavage occurs between the 3rd and 4th carbon of the substrate
- Produces glyceraldehyde-3-phosphate and forms an enamine intermediate
Tautomerization Process
- The enamine intermediate is protonated by aspartate
- Undergoes tautomerization to create a new protonated Schiff base complex
Hydrolysis of Schiff Base
- The protonated Schiff base is hydrolyzed
- Results in the release of the second product, dihydroxyacetone phosphate
- The enzyme is now free to begin a new catalytic cycle
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Description
Explore the enzymatic mechanisms of Class I aldolase through these flashcards. Each card delves into the specific steps involved in the reaction, providing insights into substrate interaction and catalytic action. Perfect for students looking to master glycolysis and enzyme function.