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6.3.5.6: asparaginyl-tRNA synthase (glutamine-hydrolysing)

This is an abbreviated version!
For detailed information about asparaginyl-tRNA synthase (glutamine-hydrolysing), go to the full flat file.

Word Map on EC 6.3.5.6

Reaction

4-phosphooxy-L-aspartyl-tRNAAsn
+
NH3
=
L-asparaginyl-tRNAAsn
 +
phosphate

Synonyms

AdT, AsnRS, Asp-AdT, Asp-tRNAAsn amidotransferase, Asp/Glu-Adt, asparaginyl-transfer RNA synthetase, Asparaginyl-tRNA synthetase, aspartyl-tRNAAsn amidotransferase, GatCAB, glutamine-dependent Asp-tRNAAsn/Glu-tRNAGln amidotransferase, NRS, tRNA-dependent amidotransferase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor
                6.3.5.6 asparaginyl-tRNA synthase (glutamine-hydrolysing)

Systematic Name

Systematic Name on EC 6.3.5.6 - asparaginyl-tRNA synthase (glutamine-hydrolysing)

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SYSTEMATIC NAME
IUBMB Comments
L-aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming)
This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis. In the first step, a non-discriminating ligase (EC 6.1.1.23, aspartate---tRNAAsn ligase) mischarges tRNAAsn with aspartate, leading to the formation of aspartyl-tRNAAsn. The aspartyl-tRNAAsn is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNAAsn (aspartyl-tRNAAsp is not a substrate for this enzyme). A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. Bacterial GatCAB complexes also has the activity of EC 6.3.5.7 (glutaminyl-tRNA synthase [glutamine-hydrolysing]).