glutamate-tRNA ligase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). [EC:6.1.1.17]

Glutamate-tRNA ligase (GluRS) is a key enzyme in protein synthesis, responsible for attaching the amino acid glutamate to its cognate tRNA molecule, tRNA(Glu). This process, known as aminoacylation, is essential for ensuring accurate translation of genetic information into proteins. GluRS plays a critical role in maintaining the fidelity of protein synthesis, as it ensures that the correct amino acid is attached to the tRNA, thereby preventing errors in the protein sequence.

GluRS catalyzes the following two-step reaction:
1. **Adenylation:** GluRS first activates glutamate by forming a high-energy adenylyl-glutamate intermediate, using ATP as an energy source.
2. **Transfer:** This activated glutamate is then transferred to the 3' end of tRNA(Glu), specifically to the 2'-hydroxyl group of the terminal adenosine residue.

The active site of GluRS is highly specific for both glutamate and tRNA(Glu), ensuring that only the correct amino acid is attached to the correct tRNA. This specificity is achieved through a combination of interactions, including hydrogen bonding, van der Waals forces, and electrostatic interactions.

In addition to its primary role in protein synthesis, GluRS has been implicated in other cellular processes, such as mRNA processing, tRNA splicing, and regulation of gene expression. Aberrant GluRS activity has been linked to various diseases, including cancer and neurodegenerative disorders.

Overall, GluRS is an essential enzyme that plays a critical role in maintaining the fidelity of protein synthesis and ensuring proper cellular function.'
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Proteins (2)

Compounds (1)