Asparaginyl-tRNA synthase (glutamine-hydrolysing)

In enzymology, an asparaginyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.6) is an enzyme that catalyzes the chemical reaction

ATP + aspartyl-tRNAAsn + L-glutamine ${\displaystyle \rightleftharpoons }$ ADP + phosphate + asparaginyl-tRNAAsn + L-glutamate

The 3 substrates of this enzyme are ATP, , and L-glutamine, whereas its 4 products are ADP, phosphate, , 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 aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Other names in common use include Asp-AdT, Asp-tRNAAsn amidotransferase, aspartyl-tRNAAsn amidotransferase, and Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming). This enzyme participates in glutamate metabolism and .

References[]

• Min B, Pelaschier JT, Graham DE, Tumbula-Hansen D, Soll D (2002). "Transfer RNA-dependent amino acid biosynthesis: an essential route to asparagine formation". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2678–83. Bibcode:2002PNAS...99.2678M. doi:10.1073/pnas.012027399. PMC 122407. PMID 11880622.
• 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. Bibcode:1998PNAS...9512838C. doi:10.1073/pnas.95.22.12838. PMC 23620. PMID 9789001.
• Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69 (1): 617–50. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471.