Difficulty: Medium
Correct Answer: Reductive amination of alpha-ketoglutarate (and related ketoacids) by specific enzymes
Explanation:
Introduction / Context:
Nitrogen assimilation is essential for biosynthesis of amino acids, nucleotides, and cofactors. Cells must convert inorganic or reduced nitrogen into organic forms. Two central enzyme systems mediate the bulk of ammonia assimilation under physiological conditions.
Given Data / Assumptions:
Concept / Approach:
Ammonia is primarily channeled into glutamate and glutamine, which then donate amino groups via transamination. Two routes dominate: (1) reductive amination of alpha-ketoglutarate by GDH to form glutamate; and (2) GS–GOGAT, where glutamine synthetase forms glutamine from glutamate + NH4+, and glutamate synthase converts glutamine + alpha-ketoglutarate into two glutamate molecules. Pyruvate is not the central acceptor for ammonia, and nitrogen fixation occurs only in specialized organisms/conditions.
Step-by-Step Solution:
Identify primary amino acceptors: alpha-ketoglutarate → glutamate; glutamate → glutamine.Recognize GDH and GS–GOGAT as main enzymatic systems.Conclude that reductive amination of alpha-ketoglutarate (and the GS–GOGAT cycle) is the major route.
Verification / Alternative check:
Biochemistry texts emphasize glutamate/glutamine as the universal nitrogen donors in biosynthesis; labeling studies trace ammonia into these pools first.
Why Other Options Are Wrong:
Common Pitfalls:
Confusing nitrogen fixation (N2 → NH4+) with assimilation (NH4+ → amino acids); they are distinct processes performed by different enzyme sets.
Final Answer:
Reductive amination of alpha-ketoglutarate (and related ketoacids) by specific enzymes
Discussion & Comments