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| EC | 6.3.5.6 | ||||||
| Accepted name: | asparaginyl-tRNA synthase (glutamine-hydrolysing) | ||||||
| Reaction: | ATP + L-aspartyl-tRNAAsn + L-glutamine + H2O = ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate (1a) L-glutamine + H2O = L-glutamate + NH3 (1b) ATP + L-aspartyl-tRNAAsn = ADP + 4-phosphooxy-L-aspartyl-tRNAAsn (1c) 4-phosphooxy-L-aspartyl-tRNAAsn + NH3 = L-asparaginyl-tRNAAsn + phosphate |
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| Other name(s): | Asp-AdT; Asp-tRNAAsn amidotransferase; aspartyl-tRNAAsn amidotransferase; Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming); aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming); GatCAB | ||||||
| Systematic name: | L-aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming) | ||||||
| Comments: | 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 Å 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]). | ||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37211-76-0 | ||||||
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