Aminolevulinate dehydratase (alad ) is an enzyme that relies on zinc as a coenzyme. a zinc ion binds to the alad active site, where it forms favorable interactions with the side chains of three amino acids. researchers have found that substituting a lead ion for a zinc ion in the alad active site causes inhibition of alad . which of the following statements best explain how the lead ion causes inhibition of alad ?
a. it changes the shape and charge of the substrate so that it becomes more compatible with alad’s active site.
b. it changes the amino acid sequence of the alad protein so that the enzyme catalyzes a different reaction.
c. it changes the three-dimensional structure of the active site so that alad is no longer compatible with its substrate.
d. it changes the enzyme-substrate complex so that the transition state is more stable and the reaction proceeds at a faster rate.
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Aminolevulinate dehydratase (alad ) is an enzyme that relies on zinc as a coenzyme. a zinc ion binds...
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