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Literature summary extracted from

  • Mandal, A.K.; Bhattacharyya, A.; Bhattacharyya, S.; Bhattacharyya, T.; Roy, S.
    A cognate tRNA specific conformational change in glutaminyl-tRNA synthetase and its implication for specificity (1998), Protein Sci., 7, 1046-1051.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.18 ATP + L-glutamine + tRNAGln Escherichia coli
-
 AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.18 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.18 ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln binding of ATP and of tRNAGln induces conformational changes that change the interaction of the enzyme with the cognate tRNA, crucial for substrate recognition and selectivity Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.18 ATP + L-glutamine + tRNAGln
-
 Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.1.1.18 additional information conformational changes are induced by tRNAGln binding not by binding of tRNAGlu Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.18 GlnRS
-
 Escherichia coli
6.1.1.18 Glutaminyl-tRNA synthetase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.18 ATP binding of ATP induces conformational changes that change the interaction of the enzyme with the cognate tRNA Escherichia coli