{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Enzyme Kinetics \u2192 Enzyme Regulation", "refinement": "This problem examines the effects of small molecules on enzyme activity, specifically focusing on Vmax and Km values.", "specific_scope": "The context involves understanding how molecules Y and Z influence the catalytic activity of enzyme Zma2 in terms of its maximum reaction rate and substrate affinity.", "goal": "Identify the roles of molecules Y and Z based on their effects on the enzyme's kinetic parameters."}, "summary": "In this problem, we analyze how two small molecules, Y and Z, affect the activity of enzyme Zma2. Molecule Y increases the enzyme's Vmax, indicating it likely enhances the enzyme's activity without affecting substrate binding, suggesting it acts as an allosteric activator. Conversely, molecule Z decreases the Km, which implies an increase in substrate affinity, characteristic of an allosteric inhibitor. Thus, the correct interpretation is that Y is an allosteric activator and Z is an allosteric inhibitor."}