EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
- |
Geobacillus stearothermophilus |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
- |
Methanothermobacter thermautotrophicus |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
- |
Helicobacter pylori |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
- |
Homo sapiens |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
Ser176A is the active-site nucleophile for facilitating Gln hydrolysis by the enzyme |
Streptococcus pyogenes |
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 |
organisms lacking Gln-tRNA synthetase produce Gln-tRNAGln from misacylated Glu-tRNAGln through the transamidation activity of Glu-tRNAGln amidotransferase. The enzyme hydrolyzes Gln to Glu and NH3, using the latter product to transamidate Glu-tRNAGln in concert with ATP hydrolysis |
Streptococcus pyogenes |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |
6.3.5.7 | ATP + Glu-tRNAGln + L-glutamine |
the enzyme produces Gln-tRNAGln required for plastidal protein biosynthesis |
Tetradesmus obliquus |
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 + L-glutamine |
GatDE is a heterodimeric amidotransferase. GatD acts as a glutaminase but only in the presence of both Glu-tRNAGln and the other subunit, GatE. The fact that only Glu-tRNAGln but not tRNA Gln could activate the glutaminase activity of GatD suggests that glutamine hydrolysis is coupled tightly to transamidation. GatE is a Glu-tRNAGln kinase that activates Glu-tRNAGln via gamma-phosphorylation |
Methanothermobacter thermautotrophicus |
ADP + phosphate + Gln-tRNAGln + L-glutamate |
- |
? |