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Literature summary for 6.1.1.17 extracted from

  • Norcum, M.T.; Dignam, J.D.
    Immunoelectron microscopic localization of glutamyl-/prolyl-tRNA synthetase within the eukaryotic multisynthetase complex (1999), J. Biol. Chem., 274, 12205-12208.
    View publication on PubMed
Search for more literature for 6.1.1.17

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + tRNAGlu Oryctolagus cuniculus
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
 enzyme has dual substrate specificity for L-glutamate and L-proline, enzyme is part of a large aminoacyl-tRNA synthetases complex
-

Source Tissue

Source Tissue Comment Organism Textmining
reticulocyte
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGlu
-
 Oryctolagus cuniculus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
ATP + L-glutamate + tRNAGlu enzyme has dual substrate specificity for L-glutamate and L-proline Oryctolagus cuniculus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
ATP + L-proline + tRNAGlu enzyme has dual substrate specificity for L-glutamate and L-proline Oryctolagus cuniculus AMP + diphosphate + L-prolyl-tRNAGlu
-
 ?

Subunits

Subunits Comment Organism
More structure and organization of the multienzyme complex Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
Glutamyl-tRNA synthetase
-
 Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Oryctolagus cuniculus