Glutaminyl-tRNA synthase (glutamine-hydrolysing)

In enzymology, a glutaminyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.7) is an enzyme that catalyzes the chemical reaction

ATP + glutamyl-tRNAGln + L-glutamine ADP + phosphate + glutaminyl-tRNAGln + L-glutamate
glutaminyl-tRNA synthase (glutamine-hydrolyzing)
Identifiers
EC number6.3.5.7
CAS number52232-48-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

The 3 substrates of this enzyme are ATP, glutamyl-tRNA(Gln), and L-glutamine, whereas its 4 products are ADP, phosphate, glutaminyl-tRNA(Gln), and L-glutamate.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming). Other names in common use include Glu-AdT, Glu-tRNAGln amidotransferase, glutamyl-tRNAGln amidotransferase, and Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming). This enzyme participates in glutamate metabolism and alanine and aspartate metabolism.

References
    • Horiuchi KY, Harpel MR, Shen L, Luo Y, Rogers KC, Copeland RA (2001). "Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase". Biochemistry. 40 (21): 6450–7. doi:10.1021/bi002599l. PMID 11371208.
    • Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D (1998). "Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 12838–43. doi:10.1073/pnas.95.22.12838. PMC 23620. PMID 9789001.
    • Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69: 617–50. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.