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. True or False.

Question

Chemistry

Averie Thomas

30 January, 11:57

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. True or False.

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Isaias Sexton · Answer 1

True

Explanation:

Aminolevulinate Dehydrogenase is one of the three enzymes required for heme biosynthesis.

The lead is responsible for inhibition of heme synthesis and it is a causative agent of haemotoxicity.

The second step of the biosynthesis of heme will be inhibited by lead activity.

The addition of lead would cause cessation in enzymatic activity as it cannot be a coenzyme instead it is an inhibitor.

The lead gets bonded to the SH group of the enzyme ceasing its function.