6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	-	-	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	a two-step reaction , in the first step, the enzyme condenses the cognate amino acid and ATP, forming an aminoacyl-adenylate intermediate with a diphosphate as the leaving group. This reaction is reversible in the absence of the tRNA. In the absence of tRNAGlu, ATP binding by GluRS is nonproductive because the alpha-phosphate of ATP and the alpha-carboxyl groups of Glu are positioned too far apart for a reaction to occur. The presence of tRNAGlu causes conformational changes surrounding the ATP binding site, allowing ATP to bind in the productive state, which moves the alpha-phosphate of the ATP closer to the alpha-carboxyl groups of Glu, allowing the reaction for the formation of the glutamyl-AMP intermediate to occur	-, 745395	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	aminoacylation reaction via a two-step mechanism involving a very unstable aa-AMP intermediate	746179	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	ATP and tRNAGlu bind randomly to the free enzyme, whereas glutamate binds only to the ternary enzyme-tRNAGlu-ATP complex. After interconversion of the quarternary enzyme-substrate complex the end-products dissociate in the order: diphosphate, AMP, Glu-tRNA	220	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	catalytic site structure, substrate binding and reaction mechanism	651000	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	concerted mechanism	212	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	random binding of ATP and L-glutamate to the enzyme-tRNA complex	-, 703636	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	the major recognition element of the tRNAGlu is U at position 34	651055	
6.1.1.17	ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	the transfer of amino acid to tRNA is accompanied by the protonation of AMP to H-AMP. Subsequent migration of proton to water reduces the stability of the complex and loosens the interface both in the presence and in the absence of AMP. The subsequent undocking of AMP or tRNA then proceeds along thermodynamically competitive pathways. Release of the tRNA acceptor stem is further accelerated by the deprotonation of the alpha-ammonium group on the charging amino acid. The proposed general base is Glu41	705182