Biochemistry—Multienzyme Complexes Tryptophan synthase of Escherichia coli is a classic bifunctional oligomeric enzyme. What is its subunit composition?

Biochemistry Enzymes Difficulty: Easy
Choose an option
  • A
    A single protein designated A only
  • B
    Two proteins designated A and B forming a functional complex
  • C
    One protein A plus an unrelated one-subunit “a” fragment
  • D
    A single protein designated B only
  • E
    Three distinct proteins designated A, B, and C

Answer

Correct Answer: Two proteins designated A and B forming a functional complex

Explanation

Introduction / Context:Many biosynthetic pathways use multienzyme complexes that channel intermediates between active sites. Tryptophan synthase is a well-studied example that couples two sequential reactions to produce tryptophan from indole-3-glycerol phosphate and serine, minimizing diffusion losses of the reactive intermediate indole.

Given Data / Assumptions:

  • Tryptophan synthase is described as bifunctional and oligomeric.
  • The canonical E. coli enzyme is known to have distinct subunits often labeled A (α) and B (β).
  • Subunits assemble into a higher-order complex for efficient catalysis.

Concept / Approach:Identify the minimal accurate description: two different subunits (A and B) associate to form the complete enzyme. This composition underlies substrate channeling: the α-subunit generates indole, which is directly delivered to the β-subunit active site for condensation with serine to form tryptophan.

Step-by-Step Solution:

Step 1: Recognize “bifunctional” implies two catalytic activities housed in distinct subunits.Step 2: Recall the established α2β2 architecture in many organisms; the essential point is the presence of A and B subunits.Step 3: Select the option that explicitly states “two proteins designated A and B.”

Verification / Alternative check:Structural and kinetic studies show inter-subunit tunnels guiding indole from A to B, consistent with the AB composition.

Why Other Options Are Wrong:

  • Only A or only B: would delete half the catalytic function.
  • “A plus one-subunit a”: nonstandard and incorrect nomenclature.
  • Three proteins A, B, C: not supported for the classic bacterial enzyme.

Common Pitfalls:Confusing the two-subunit composition with other multienzyme assemblies that include additional regulatory subunits; conflating stoichiometry details with the essential identity of A and B.

Final Answer:Two proteins designated A and B forming a functional complex

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