BRENDA - Enzyme Database

Mutagenesis and mechanism-based inhibition of Streptococcus pyogenes Glu-tRNAGln amidotransferase implicate a serine-based glutaminase site

Harpel, M.R.; Horiuchi, K.Y.; Luo, Y.; Shen, L.; Jiang, W.; Nelson, D.J.; Rogers, K.C.; Decicco, C.P.; Copeland, R.A.; Biochemistry 41, 6398-6407 (2002)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
6.3.5.7
gamma-Glu boronic acid
IC50: 0.0016 mM
Streptococcus pyogenes
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.3.5.7
Streptococcus pyogenes
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.5.7
ATP + Glu-tRNAGln + L-glutamine
Ser176A is the active-site nucleophile for facilitating Gln hydrolysis by the enzyme
492304
Streptococcus pyogenes
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
492304
Streptococcus pyogenes
?
IC50 Value
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
6.3.5.7
0.0016
-
IC50: 0.0016 mM
Streptococcus pyogenes
gamma-Glu boronic acid
IC50 Value (protein specific)
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
6.3.5.7
0.0016
-
IC50: 0.0016 mM
Streptococcus pyogenes
gamma-Glu boronic acid
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
6.3.5.7
gamma-Glu boronic acid
IC50: 0.0016 mM
Streptococcus pyogenes
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.5.7
ATP + Glu-tRNAGln + L-glutamine
Ser176A is the active-site nucleophile for facilitating Gln hydrolysis by the enzyme
492304
Streptococcus pyogenes
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
492304
Streptococcus pyogenes
?