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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the reaction diagram Show all sequences 6.1.1.B3ATP + L-glutamate + tRNA acceptor is unfractionated RNA Escherichia coli AMP + diphosphate + L-glutamyl-tRNA the activation step of L-glutamate is tRNA-independent ?
Display the reaction diagram Show all sequences 6.1.1.B3ATP + L-glutamate + tRNAAsp - Shigella flexneri AMP + diphosphate + L-glutamyl-tRNAAsp - ?
Display the reaction diagram Show all sequences 6.1.1.B3ATP + L-glutamate + tRNAAsp - Escherichia coli AMP + diphosphate + L-glutamyl-tRNAAsp - ?
Display the reaction diagram Show all sequences 6.1.1.B3ATP + L-glutamate + tRNAAsp enzyme YadB activates glutamate in the absence of tRNA and transfers the activated glutamate not on tRNAGlu but instead on tRNAAsp. tRNAAsp is able to accept two amino acids: aspartate charged by aspartyl-tRNA synthetase and glutamate charged byYadB. YadB transfers the activated glutamate on the cyclopenthene-diol ring of the modified nucleoside queuosine posttranscriptionally inserted at the wobble position of the anticodon-loop to form glutamylqueuosine Escherichia coli AMP + diphosphate + L-glutamyl-tRNAAsp - ?
Display the reaction diagram Show all sequences 6.1.1.B3ATP + L-glutamate + tRNAAsp the enzyme glutamylates the queuosine Q34 nucleotide of the anticodon of tRNAAsp Escherichia coli AMP + diphosphate + L-glutamyl-tRNAAsp - ?
Display the reaction diagram Show all sequences 6.1.1.B3ATP + L-glutamate + tRNAAsp - Shigella flexneri 2457T / ATCC 700930 AMP + diphosphate + L-glutamyl-tRNAAsp - ?
Display the reaction diagram Show all sequences 6.1.1.B3more among Escherichia coli tRNAs containing queuosine in the wobble position, only tRNAAsp is substrate ofYadB. No substrate: D-glutamate Escherichia coli ? - ?
Display the reaction diagram Show all sequences 6.1.1.B3more enzyme does not catalyse attachment of the activated L-glutamate to Escherichia coli tRNAGlu Escherichia coli ? - ?
Display the reaction diagram Show all sequences 6.1.1.B3more Glu-Q-RS glutamylates the Q34 residue of the anticodon of tRNAAsp, hence it is a tRNA hypermodifying enzyme Escherichia coli ? - ?
Display the reaction diagram Show all sequences 6.1.1.B3more the enzyme cannot aminoacylate tRNAGlu in vitro Escherichia coli ? - ?
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