EC Number   |
Natural Substrates |
|---|
    6.1.1.24 | ATP + L-Glu + tRNAGln |
- |
| 6.1.1.24 | ATP + L-glutamate + tRNAAsp |
the L-glutamyl-queuosine tRNAAsp synthetase, Glu-Q-RS from Escherichia coli is a paralogue of the catalytic core of glutamyl-tRNA synthetase, GluRS, that catalyzes glutamylation of queuosine in the wobble position of tRNAAsp |
| 6.1.1.24 | ATP + L-glutamate + tRNAGln |
- |
| 6.1.1.24 | ATP + L-glutamate + tRNAGln |
tRNAGln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase |
| 6.1.1.24 | ATP + L-glutamate + tRNAGlu |
- |
| 6.1.1.24 | ATP + L-glutamate + tRNAGlx |
- |
| 6.1.1.24 | ATP + L-glutamate + tRNAGlx |
the enzyme is capable of mischarging plastidal tRNAGln from barley with glutamate as well as regularly charges the plastidal tRNAGlu from Scenedesmus. The mischarged glutamyl-tRNAGln is subsequently amidated by glutamyl-tRNA amidotransferase to form the glutaminyl-tRNAGln required for plastidal protein biosynthesis |
| 6.1.1.24 | ATP + L-glutamate + tRNAGlx |
the enzyme aminoacylates both tRNAGlu and tRNAGln because Rhizobium meliloti contains no glutaminyl-tRNAGln ligase |
| 6.1.1.24 | ATP + L-glutamate + tRNAGlx |
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis |
| 6.1.1.24 | more |
ND-GluRS recognizes both tRNAGlu and tRNAGln without significantly discriminating between them, tRNA discrimination module, overview. The first point of significant distinction between the GlnRS and ND-GluRS tRNA recognition involves residues contacting the G36 nucleobase. A second distiction involves a beta-hairpin module in the CP domain |
