Asparaginyl-tRNA synthase (glutamine-hydrolysing)

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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 $\rightleftharpoons$ ADP + phosphate + asparaginyl-tRNAAsn + L-glutamate

The 3 substrates of this enzyme are ATP, aspartyl-tRNA(Asn), and L-glutamine, whereas its 4 products are ADP, phosphate, asparaginyl-tRNA(Asn), 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 alanine and aspartate metabolism.

[edit] References

IUBMB entry for 6.3.5.6
BRENDA references for 6.3.5.6 (Recommended.)
PubMed references for 6.3.5.6
PubMed Central references for 6.3.5.6
Google Scholar references for 6.3.5.6
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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: 12838–43. doi:10.1073/pnas.95.22.12838. 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.