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Literature summary for 2.4.2.14 extracted from

  • Zhou, G.; Charbonneau, H.; Colman, R.F.; Zalkin, H.
    Identification of sites for feedback regulation of glutamine 5-phosphoribosylpyrophosphate amidotransferase by nucleotides and relationship to residues important for catalysis (1993), J. Biol. Chem., 268, 10471-10481.
    View publication on PubMed
Search for more literature for 2.4.2.14

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type, Y74A, Y258A, Y258F, K326Q, Y329A, G331I, N351A and Y465A mutant enzyme in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
G331I 50% of wild-type glutaminase activity, reduced inhibition by GMP, enhanced inhibition by AMP Escherichia coli
K326Q similar glutaminase and amidotransferase activity as wild-type, not inhibited by GMP Escherichia coli
N351A approx. 50% of wild-type glutaminase activity, completely insensitive to inhibition by GMP, partially resistent to inhibition by AMP Escherichia coli
Y258A complete loss of glutaminase and amidotransferase activity Escherichia coli
Y258F approx. 50% loss of glutaminase activity, very weak amidotransferase activity Escherichia coli
Y329A normal glutaminase activity, approx. 20% amidotransferase activity, less sensitive to GMP inhibition than wild-type Escherichia coli
Y465A 100% of wild-type glutaminase activity, 28% of wild-type amidotransferase activity, inhibition by GMP and AMP is similar to wild-type Escherichia coli
Y74A complete loss of glutaminase activity, little loss of amidotransferase activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5'-p-fluorosulfonylbenzoyladenosine inactivation follows pseudo-first order kinetic, AMP, GMP and 5-phospho-alpha-D-ribose 1-diphosphate protect Escherichia coli
AMP 4.7 mM, 50% inhibition Escherichia coli
GMP 1.2-1.4 mM, 50% inhibition Escherichia coli
additional information synergistic inhibition of glutaminase activity by AMP plus GMP and N3-AMP plus GMP Escherichia coli
N3-AMP 1.2-1.4 mM, 50% inhibition, AMP and GMP protect Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.39
-
 5'-p-fluorosulfonylbenzoyladenosine
-
 Escherichia coli