EC Number |
Reaction |
Reference |
---|
6.1.1.18 | ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln |
- |
- |
6.1.1.18 | ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln |
active site residues are Tyr240 and Phe90 |
651246 |
6.1.1.18 | ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln |
aminoacylation reaction mechanism, substrate binding sites, Tyr211 and a water molecule are responsible for recognition of both hydrogen atoms of the nitrogen of glutamine sidechain, which is esstial for substrate recognition |
653922 |
6.1.1.18 | ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln |
binding of ATP and of tRNAGln induces conformational changes that change the interaction of the enzyme with the cognate tRNA, crucial for substrate recognition and selectivity |
653817 |
6.1.1.18 | ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln |
structurefunction relationship, overview |
-, 676219 |