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Literature summary extracted from

  • Strauch, M.A.; Zalkin, H.; Aronson, A.I.
    Characterization of the glutamyl-tRNAGln-to-glutaminyl-tRNAGln amidotransferase reaction of Bacillus subtilis (1988), J. Bacteriol., 170, 916-920.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.7 L-methionine-S-sulfoximine at 1 mM, 3 mM or 5 mM, 20% inhibition Bacillus subtilis
6.3.5.7 additional information no inhibition by 6-diazo-5-oxonorleucine Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.7 0.01
-
Gln
-
Bacillus subtilis
6.3.5.7 0.1 0.2 Asn
-
Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.7 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 + NH4Cl NH4Cl is much less effective as amide donor than glutamine Bacillus subtilis ADP + phosphate + Gln-tRNAGln + ?
-
?