Biology:Glutamate—tRNA(Gln) ligase
From HandWiki
| Glutamate—tRNAGln ligase | |||||||||
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| Identifiers | |||||||||
| EC number | 6.1.1.24 | ||||||||
| CAS number | 9068-76-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glutamate—tRNAGln ligase (EC 6.1.1.24) is an enzyme that catalyzes the chemical reaction
- ATP + L-glutamate + tRNAGlx [math]\displaystyle{ \rightleftharpoons }[/math] AMP + diphosphate + glutamyl-tRNAGlx
The 3 substrates of this enzyme are ATP, L-glutamate, and tRNAGlx, whereas its 3 products are AMP, diphosphate, and glutamyl-tRNAGlx.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-glutamate:tRNAGlx ligase (AMP-forming). This enzyme is also called glutamyl-tRNA synthetase. This enzyme participates in glutamate metabolism.
References
- "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69: 617–50. 2000. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471.
- "Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation". EMBO J. 17 (17): 5227–37. 1998. doi:10.1093/emboj/17.17.5227. PMID 9724658.
- "Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl-tRNA synthetase". Mol. Cells 8 (4): 459–65. 1998. PMID 9749534.
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