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PMID:6280993
| Citation |
Kern, D and Lapointe, J (1980) The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. Evidence for a two-step aminoacylation pathway, and study of the reactivity of the intermediate complex. Eur. J. Biochem. 106:137-50 |
|---|---|
| Abstract |
No abstract in PubMed |
| Links | |
| Keywords |
Adenosine Monophosphate/metabolism; Adenosine Triphosphate/metabolism; Amino Acyl-tRNA Synthetases/metabolism; Catalysis; Diphosphates/metabolism; Escherichia coli/enzymology; Glutamate-tRNA Ligase/metabolism; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines/pharmacology; Kinetics; Models, Chemical; RNA, Transfer, Amino Acyl/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
NOT |
GO:0004818: glutamate-tRNA ligase activity |
ECO:0000314: |
F |
Table 4 and Fig. 4 shows that GluRS can bind both ATP and its tRNA substrate independently, but binding of glutamate requires the presence of tRNAGlu. |
complete | |||
See also
References
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