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Literature summary extracted from

  • Harpel, M.R.; Horiuchi, K.Y.; Luo, Y.; Shen, L.; Jiang, W.; Nelson, D.J.; Rogers, K.C.; Decicco, C.P.; Copeland, R.A.
    Mutagenesis and mechanism-based inhibition of Streptococcus pyogenes Glu-tRNAGln amidotransferase implicate a serine-based glutaminase site (2002), Biochemistry, 41, 6398-6407.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.7 gamma-Glu boronic acid IC50: 0.0016 mM Streptococcus pyogenes

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.7 Streptococcus pyogenes
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.7 ATP + Glu-tRNAGln + L-glutamine Ser176A is the active-site nucleophile for facilitating Gln hydrolysis by the enzyme Streptococcus pyogenes ADP + phosphate + Gln-tRNAGln + L-glutamate
-
 ?

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
6.3.5.7 0.0016
-
 IC50: 0.0016 mM Streptococcus pyogenes gamma-Glu boronic acid