Literature summary for 6.3.5.6 extracted from

Bernard, D.; Akochy, P.M.; Bernier, S.; Fisette, O.; Brousseau, O.C.; Chenevert, R.; Roy, P.H.; Lapointe, J.
Inhibition by L-aspartol adenylate of a nondiscriminating aspartyl-tRNA synthetase reveals differences between the interactions of its active site with tRNAAsp and tRNAAsn (2007), J. Enzyme Inhib. Med. Chem., 22, 77-82.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + Asp-tRNA + L-Gln	in presence of tRNA-dependent amidotransferase AdT, amidation activity	Pseudomonas aeruginosa	?	-	?
additional information	a nondiscriminating aspartyl-tRNA synthetase, ND-DRS, first generates a mischarged aspartyl-tRNAAsn that dissociates from the enzyme and binds to a tRNA-dependent amidotransferase, AdT, which then converts the tRNA-bound aspartate into asparagine, the ND-DRS, tRNAAsn, and AdT assemble into a specific ribonucleoprotein complex called transamidosome that remains stable during the overall catalytic process, overview	Pseudomonas aeruginosa	?	-	?

Synonyms

Synonyms	Comment	Organism
tRNA-dependent amidotransferase	-	Pseudomonas aeruginosa

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)