Glutamine—tRNA ligase

In enzymology, a glutamine—tRNA ligase (EC 6.1.1.18) is an enzyme that catalyzes the chemical reaction

ATP + L-glutamine + tRNAGln AMP + diphosphate + L-glutaminyl-tRNAGln
Glutamine—tRNA ligase
Identifiers
EC no.6.1.1.18
CAS no.9075-59-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The 3 substrates of this enzyme are ATP, L-glutamine, and tRNA(Gln), whereas its 3 products are AMP, diphosphate, and L-glutaminyl-tRNA(Gln).

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-glutamine:tRNAGln ligase (AMP-forming). Other names in common use include glutaminyl-tRNA synthetase, glutaminyl-transfer RNA synthetase, glutaminyl-transfer ribonucleate synthetase, glutamine-tRNA synthetase, glutamine translase, glutamate-tRNA ligase, glutaminyl ribonucleic acid, and GlnRS. This enzyme participates in glutamate metabolism and aminoacyl-trna biosynthesis.

Structural studies

As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes 1EUQ, 1EUY, 1EXD, 1GSG, 1GTR, 1GTS, 1NYL, 1O0B, 1O0C, 1QRS, 1QRT, 1QRU, 1QTQ, 1ZJW, and 2HZ7.

References

    • Ravel JM, Wang S, Heinemeyer C, Shive W (1965). "Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia coli W. Separation, properties, and stimulation of adenosine triphosphate-pyrophosphate exchange by acceptor ribonucleic acid". J. Biol. Chem. 240: 432–438. PMID 14253448.


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