Aminoacyltransferase

From WikiMD's Food, Medicine & Wellness Encyclopedia

Aminoacyltransferase is an enzyme that plays a crucial role in the process of protein synthesis. It is responsible for the attachment of an amino acid to its corresponding transfer RNA (tRNA), a process known as aminoacylation or tRNA charging. This process is essential for the translation of genetic code into proteins.

Function[edit | edit source]

Aminoacyltransferase catalyzes the esterification of a specific amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. This process occurs in two steps:

  1. The amino acid is first activated by ATP to form an aminoacyl-adenylate.
  2. The enzyme then transfers the amino acid to the tRNA, forming an aminoacyl-tRNA.

This reaction ensures that the correct amino acid is added to the growing polypeptide chain during protein synthesis.

Structure[edit | edit source]

Aminoacyltransferases are typically composed of multiple subunits and have a complex three-dimensional structure. The active site of the enzyme, where the aminoacylation reaction takes place, is usually located in a cleft between the subunits.

Clinical significance[edit | edit source]

Mutations in the genes encoding aminoacyltransferases can lead to a variety of diseases. For example, defects in the enzyme alanyl-tRNA synthetase can cause neurological disorders such as Charcot-Marie-Tooth disease.

See also[edit | edit source]

References[edit | edit source]


Wiki.png

Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD


Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro) available.
Advertise on WikiMD

WikiMD is not a substitute for professional medical advice. See full disclaimer.

Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.


Contributors: Prab R. Tumpati, MD