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Literature summary for 6.3.5.7 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
Search for more literature for 6.3.5.7

Cloned(Commentary)

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bacillus subtilis

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Glu-tRNAGln + Asn Asn is much less effective as amide donor than glutamine Bacillus subtilis ADP + phosphate + Gln-tRNAGln + Asp
-
 ?
ATP + Glu-tRNAGln + L-glutamine
-
 Bacillus subtilis ADP + phosphate + Gln-tRNAGln + L-glutamate
-
 ?
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
-
 ?
ATP + Glu-tRNAGln + NH4Cl NH4Cl is much less effective as amide donor than glutamine Bacillus subtilis ADP + phosphate + Gln-tRNAGln + ?
-
 ?

Subunits

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