Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Curnow, A.W.; Hong, K.W.; Yuan, R.; Kim, S.I.; Martins, O.; Winkler, W.; Henkin, T.M.; Soll, D.
    Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation (1997), Proc. Natl. Acad. Sci. USA, 94, 11819-11826.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.5.7 cloning of the three genes, gatC, gatA, and gatB, which constitute the transcriptional unit of the enzyme Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.5.7 Mg2+ required Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.5.7 10900
-
 1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE Bacillus subtilis
6.3.5.7 53000
-
 1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE Bacillus subtilis
6.3.5.7 53500
-
 1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.5.7 ATP + Glu-tRNAGln + L-glutamine Bacillus subtilis disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles ADP + phosphate + Gln-tRNAGln + L-glutamate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.7 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.5.7
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.5.7 0.009
-
-
 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.7 ATP + Glu-tRNAGln + Asn Asn is much less effective as amide donor than glutamine Bacillus subtilis ADP + phosphate + Gln-tRNAGln + Asp
-
 ?
6.3.5.7 ATP + Glu-tRNAGln + L-glutamine
-
 Bacillus subtilis ADP + phosphate + Gln-tRNAGln + L-glutamate
-
 ?
6.3.5.7 ATP + Glu-tRNAGln + L-glutamine disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles Bacillus subtilis ADP + phosphate + Gln-tRNAGln + L-glutamate
-
 ?
6.3.5.7 ATP + Glu-tRNAGln + NH4Cl NH4Cl is much less effective as amide donor than glutamine Bacillus subtilis ADP + phosphate + Gln-tRNAGln + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.7 trimer 1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE Bacillus subtilis