"Glutamyl tRNA Synthetase" is a challenging term to spell due to its complex combination of letters and sounds. Its pronunciation is [ɡluːtəmɪl tiː ɑːr ɛn əʊ ˈsɪnθəseɪz]. The "glutamyl" part starts with a hard G and ends with a long E vowel sound. The "tRNA" part is pronounced with a silent N before the A vowel sound, and the final "synthetase" ends with a long E sound following the S and TH consonant blends. Phonetic transcription helps to understand how sounds are represented in written language and improve spelling accuracy.
Glutamyl tRNA synthetase is an enzyme that plays a crucial role in protein synthesis. It is responsible for attaching the amino acid glutamine to its corresponding transfer RNA (tRNA) molecule during the process of translation in cells.
The enzyme follows a precise mechanism to ensure accurate attachment of glutamine to tRNA. It recognizes the specific tRNA molecule for glutamine, called tRNA-Gln, and forms a stable complex with it. Glutamine is activated by the enzyme through the hydrolysis of ATP (adenosine triphosphate) to produce ADP (adenosine diphosphate) and an AMP (adenosine monophosphate)-linked glutamine molecule.
Once activated, the glutamine molecule is transferred from the enzyme to the tRNA-Gln molecule, forming a bond between the amino acid and ribose residue within the tRNA. This specific attachment is essential for the subsequent incorporation of glutamine into growing polypeptide chains during protein synthesis.
Glutamyl tRNA synthetase is found in all living organisms and is highly conserved throughout evolution, highlighting its vital role in cellular processes. Mutations in the gene encoding this enzyme can impair protein synthesis, leading to various diseases and disorders.
In summary, glutamyl tRNA synthetase is an enzyme responsible for attaching the amino acid glutamine to its corresponding tRNA molecule, ensuring accurate translation of genetic information into protein synthesis.