Step 1: Understanding the Question:
The question asks about the metabolic consequences of completely inhibiting the enzyme pyruvate dehydrogenase (PDH) in a cell.
Step 2: Detailed Explanation:
• Pyruvate dehydrogenase (PDH) is a key mitochondrial enzyme complex that catalyzes the link reaction.
• This reaction converts pyruvate (produced via glycolysis in the cytoplasm) into acetyl-coenzyme A (acetyl-CoA) in the mitochondrial matrix.
• Acetyl-CoA is the primary input molecule for the tricarboxylic acid (TCA) cycle (Krebs cycle).
• When PDH is completely inhibited, pyruvate cannot be converted into acetyl-CoA, effectively blocking the aerobic respiration pathway.
• As aerobic metabolism halts, the cell must rely solely on anaerobic glycolysis to produce adenosine triphosphate (ATP).
• However, glycolysis requires a continuous supply of oxidized nicotinamide adenine dinucleotide ($\text{NAD}^+$) to convert glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate.
• Under aerobic conditions, $\text{NAD}^+$ is regenerated by the electron transport chain (ETC) in the mitochondria.
• Without PDH and aerobic respiration, the cell must regenerate $\text{NAD}^+$ anaerobically through lactate fermentation, where lactate dehydrogenase reduces pyruvate to lactate while oxidizing NADH back to $\text{NAD}^+$.
• This anaerobic pathway allows glycolysis to continue, producing a net yield of 2 ATP per glucose molecule.
Step 3: Final Answer:
Therefore, glycolysis continues with $\text{NAD}^+$ regeneration via lactate fermentation, yielding 2 ATP per glucose molecule.