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Chapter 15: Q7. (page 497)

Why is triose phosphate isomerase considered to be catalytically perfect?

Short Answer

Expert verified

Triose phosphate isomerase is considered catalytically perfect because of its kcat/Km value which is in the diffusion-limit range.

Step by step solution

01

Role of triose phosphate isomerase

During glycolysis, the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (GAP) is catalyzed by triose-phosphate isomerase.

02

Triose phosphate isomerase is considered catalytically perfect

Triose phosphate isomerase is a catalytically perfect enzyme because its kcat/Km value is in the diffusion-limited range. The product formation happens as soon as the enzyme and its substrate collide in the solution. As a result, any improvement in the enzyme's catalytic efficiency will not enhance its reaction rate.

The concentrations of GAP and DHAP are kept at their equilibrium values because they are interconverted so efficiently by triose phosphate isomerase.

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Most popular questions from this chapter

How does flux through the pentose phosphate pathway change in response to the need for NADPH or ribose-5-phosphate?

Why is it possible for the 鈭咷 values in Table 15-1 to differ from the 鈭咷掳藞 values?

Some bacteria catabolize glucose by the Entner-Doudoroff pathway, a variant of glycolysis in which glucose-6-phosphate is convertedto 6-phosphogluconate (as in the pentose phosphate pathway) and thento 2-keto-3-deoxy-6-phosphogluconate (KDPG).

Next, an aldolase acts on KDPG. (a) Draw the structures of the products of the KDPG aldolase reaction. (b) Describe how these reaction products are further metabolized by glycolytic enzymes. (c) What isthe ATP yield when glucose is metabolized to pyruvate by the Entner-Doudoroff pathway? How does this compare to the ATP yield of glycolysis?

Question: Under standard conditions, is the oxidation of free FADH2 by ubiquinone sufficiently exergonic to drive the synthesis of ATP?

When the pathogen Salmonella typhimurium infects mammalian cells, the host cell protease caspase-1 is enabled to cleave and thereby activate signaling proteins that instigate the immune response. The targets of caspase-1 also include aldolase and enolase. What effect would this have on the infected cell and why might this be advantageous to the organism?
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