EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
6.3.5.7 | ATP + Asp-tRNAAsn + L-glutamine |
- |
Acidithiobacillus ferrooxidans |
ADP + phosphate + Asn-tRNAAsn + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
- |
Acidithiobacillus ferrooxidans |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + Asn |
Asn is much less effective as amide donor than glutamine |
Bacillus subtilis |
ADP + phosphate + Gln-tRNAGln + Asp |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-asparagine |
- |
Bacillus subtilis |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
- |
Bacillus subtilis |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
the amidation of Glu-tRNAGln proceeds via a gamma-phosphorylated intermediate |
Bacillus subtilis |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles |
Bacillus subtilis |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + NH4Cl |
NH4Cl is much less effective as amide donor than glutamine |
Bacillus subtilis |
ADP + phosphate + Gln-tRNAGln + ? |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + Asn |
- |
Chlamydomonas reinhardtii |
ADP + phosphate + Gln-tRNAGln + Asp |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
- |
Chlamydomonas reinhardtii |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |