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Literature summary extracted from

  • Horiuchi, K.Y.; Harpel, M.R.; Shen, L.; Luo, Y.; Rogers, K.C.; Copeland, R.A.
    Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase (2001), Biochemistry, 40, 6450-6457.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.5.7 additional information activation of glutaminase activity by ATP or ATP-gammaS together with Glu-tRNAGln, results either from an allosteric effect due simply to binding of these analogues to the enzyme or from some structural changes that attend ATP or ATP-gammaS hydrolysis Streptococcus pyogenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.7 2'-O-(trinitrophenyl)adenosine 5'-triphosphate IC50: 2.4 mM Streptococcus pyogenes
6.3.5.7 3'-O-(trinitrophenyl)adenosine 5'-triphosphate IC50: 2.4 mM Streptococcus pyogenes
6.3.5.7 adenosine 5'-[beta,gamma-methylene]triphosphate IC50: 2.3 mM Streptococcus pyogenes
6.3.5.7 ADP IC50: 0.026 mM Streptococcus pyogenes
6.3.5.7 ATP-gammaS IC50: 0.19 mM Streptococcus pyogenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.7 0.0002
-
 L-glutamyl-tRNAGlu
-
 Streptococcus pyogenes
6.3.5.7 0.0159
-
 Gln
-
 Streptococcus pyogenes
6.3.5.7 0.117
-
 ATP
-
 Streptococcus pyogenes

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 Streptococcus pyogenes organisms lacking Gln-tRNA synthetase produce Gln-tRNAGln from misacylated Glu-tRNAGln through the transamidation activity of Glu-tRNAGln amidotransferase. The enzyme hydrolyzes Gln to Glu and NH3, using the latter product to transamidate Glu-tRNAGln in concert with ATP hydrolysis ADP + phosphate + Gln-tRNAGln + L-glutamate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.7 Streptococcus pyogenes
-
 recombinant enzyme expressed in Escherichia coli
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.7 ATP + Glu-tRNAGln + L-glutamine organisms lacking Gln-tRNA synthetase produce Gln-tRNAGln from misacylated Glu-tRNAGln through the transamidation activity of Glu-tRNAGln amidotransferase. The enzyme hydrolyzes Gln to Glu and NH3, using the latter product to transamidate Glu-tRNAGln in concert with ATP hydrolysis Streptococcus pyogenes ADP + phosphate + Gln-tRNAGln + L-glutamate
-
 ?
6.3.5.7 ATP-gammaS + Glu-tRNAGln + L-glutamine
-
 Streptococcus pyogenes ? + phosphate + Gln-tRNAGln + L-glutamate
-
 ?
6.3.5.7 additional information in absence of the amido acceptor, Glu-tRNAGln, the enzyme has basal glutaminase activity that is unaffected by ATP Streptococcus pyogenes ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.5.7 0.51
-
 Gln
-
 Streptococcus pyogenes
6.3.5.7 0.59
-
 ATP
-
 Streptococcus pyogenes

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
6.3.5.7 0.026
-
 IC50: 0.026 mM Streptococcus pyogenes ADP
6.3.5.7 0.19
-
 IC50: 0.19 mM Streptococcus pyogenes ATP-gammaS
6.3.5.7 2.3
-
 IC50: 2.3 mM Streptococcus pyogenes adenosine 5'-[beta,gamma-methylene]triphosphate
6.3.5.7 2.4
-
 IC50: 2.4 mM Streptococcus pyogenes 2'-O-(trinitrophenyl)adenosine 5'-triphosphate
6.3.5.7 2.4
-
 IC50: 2.4 mM Streptococcus pyogenes 3'-O-(trinitrophenyl)adenosine 5'-triphosphate