Question:
Transfer of an amino group from an amino acid to an alpha-keto acid is done by which enzyme?
Transfer of an amino group from an amino acid to an alpha-keto acid is done by which enzyme?
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Moving an amino group between an amino acid and a keto acid is transamination.
Updated On: Jun 24, 2026
- Transaminases
- Aminases
- Transketolase
- Decarboxylase
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The Correct Option is A
Solution and Explanation
Step 1: Read the reaction described. An amino group is being moved from an amino acid onto an alpha-keto acid, converting the keto acid into a new amino acid.
Step 2: Name the reaction type. This swap of an amino group between an amino acid and a keto acid is called transamination.
Step 3: Identify the enzyme class. Transamination is catalyzed by transaminases (aminotransferases), such as ALT (alanine aminotransferase) and AST (aspartate aminotransferase).
Step 4: Note the cofactor. These enzymes require pyridoxal phosphate (vitamin B6) as the amino-group carrier.
Step 5: Exclude the others. Transketolase transfers two-carbon units in the pentose phosphate pathway, decarboxylases remove carboxyl groups as CO2, and aminases is not a standard enzyme class for this reaction.
Conclusion: The enzyme is a transaminase, so the correct answer is option 1.
Step 2: Name the reaction type. This swap of an amino group between an amino acid and a keto acid is called transamination.
Step 3: Identify the enzyme class. Transamination is catalyzed by transaminases (aminotransferases), such as ALT (alanine aminotransferase) and AST (aspartate aminotransferase).
Step 4: Note the cofactor. These enzymes require pyridoxal phosphate (vitamin B6) as the amino-group carrier.
Step 5: Exclude the others. Transketolase transfers two-carbon units in the pentose phosphate pathway, decarboxylases remove carboxyl groups as CO2, and aminases is not a standard enzyme class for this reaction.
Conclusion: The enzyme is a transaminase, so the correct answer is option 1.
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