ASP TRNA LIGASE Meaning and
Definition
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Asp tRNA Ligase, or aspartyl-tRNA synthetase, is an enzyme responsible for the critical process of aminoacylation in protein synthesis. It specifically catalyzes the attachment of the amino acid aspartic acid (Asp) to its corresponding transfer RNA (tRNA) molecule, resulting in the formation of aspartyl-tRNA.
The role of Asp tRNA Ligase is essential in ensuring accurate translation of the genetic code during protein synthesis. This enzyme recognizes the specific tRNA molecule carrying aspartic acid and covalently attaches the amino acid to the tRNA's terminal adenosine residue. This aminoacylation process is essential for successful assembly of polypeptide chains and subsequent protein formation.
Asp tRNA Ligase exhibits specificity for aspartic acid, ensuring that this particular amino acid is correctly paired with its corresponding tRNA molecule. Through a series of chemical reactions, Asp tRNA Ligase utilizes adenosine triphosphate (ATP) as a source of energy to activate the aspartic acid, and then transfers it onto the tRNA.
In summary, Asp tRNA Ligase is an enzyme that plays a crucial role in protein synthesis by catalyzing the attachment of aspartic acid to its corresponding tRNA molecule, forming aspartyl-tRNA. This enzyme ensures accuracy and fidelity in translation by specifically recognizing aspartic acid and pairing it with the correct tRNA molecule.
Common Misspellings for ASP TRNA LIGASE
- zsp trna ligase
- ssp trna ligase
- wsp trna ligase
- qsp trna ligase
- aap trna ligase
- azp trna ligase
- axp trna ligase
- adp trna ligase
- aep trna ligase
- awp trna ligase
- aso trna ligase
- asl trna ligase
- as- trna ligase
- as0 trna ligase
- asp rrna ligase
- asp frna ligase
- asp grna ligase
- asp yrna ligase
- asp 6rna ligase
- asp 5rna ligase
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