How does a non-competitive inhibitor change enzyme kinetics?
ARaises Km, Vmax unchanged
BLowers Vmax, Km unchanged
CRaises both Km and Vmax
DLowers Km, Vmax unchanged
Answer & Solution
Correct answer: B. Lowers Vmax, Km unchanged
It binds away from the substrate site, so substrate affinity and Km stay the same while Vmax falls.
Keep practising Biomolecules
Browse all Biomolecules questions for NEET UG, or explore more Biology topics.
Related questions
What effect do enzymes have on a reaction's equilibrium position?Which enzyme is used in meat tenderizers?What does the turnover number kcat measure?What does the Michaelis constant Km represent?What name did Eduard Buchner give the enzyme fermenting sucrose in yeast extract?Which metal ion is a cofactor of carboxypeptidase?Coenzymes NAD and NADP contain which vitamin?How do prosthetic groups differ from other cofactors?