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Literature summary for 6.1.1.18 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)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
GlnRS
-
Escherichia coli
Glutaminyl-tRNA synthetase
-
Escherichia coli

Cofactor

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