Aminoacyltransferase

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Aminoacyltransferase[edit | edit source]

General structure of an amine, a key component in aminoacyltransferase reactions.

Aminoacyltransferase is an enzyme that plays a crucial role in the process of protein synthesis by facilitating the transfer of an amino acid to a tRNA molecule. This enzyme is essential for the accurate translation of the genetic code into functional proteins.

Function[edit | edit source]

Aminoacyltransferases are responsible for catalyzing the attachment of an amino acid to its corresponding tRNA, a process known as "aminoacylation" or "charging" of tRNA. This reaction is vital for the translation of mRNA into a polypeptide chain during protein synthesis. The enzyme ensures that each tRNA is linked to the correct amino acid, maintaining the fidelity of the genetic code.

Mechanism[edit | edit source]

The mechanism of action of aminoacyltransferase involves two main steps:

  1. Activation of the amino acid: The enzyme first activates the amino acid by forming an aminoacyl-adenylate intermediate, using ATP as a cofactor.
  2. Transfer to tRNA: The activated amino acid is then transferred to the 3' end of the tRNA molecule, forming an aminoacyl-tRNA complex.

This two-step reaction is crucial for the high specificity and accuracy of protein synthesis.

Types[edit | edit source]

There are two main classes of aminoacyltransferases, classified based on their structural and functional characteristics:

  • Class I aminoacyltransferases: These enzymes typically attach the amino acid to the 2'-OH group of the terminal adenosine of tRNA.
  • Class II aminoacyltransferases: These enzymes attach the amino acid to the 3'-OH group of the terminal adenosine of tRNA.

Each class has distinct structural motifs and catalytic mechanisms, reflecting their evolutionary divergence.

Importance in Biology[edit | edit source]

Aminoacyltransferases are essential for the proper functioning of the ribosome during protein synthesis. Errors in aminoacylation can lead to the incorporation of incorrect amino acids into proteins, potentially resulting in dysfunctional proteins and diseases. Therefore, these enzymes are critical for maintaining cellular homeostasis and organismal health.

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Contributors: Prab R. Tumpati, MD