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Literature summary for 2.4.2.14 extracted from

  • Kim, J.H.; Wolle, D.; Haridas, K.; Parry, R.J.; Smith, J.L.; Zalkin, H.
    A stable carbocyclic analog of 5-phosphoribosyl-1-pyrophosphate to probe the mechanism of catalysis and regulation of glutamine phosphoribosylpyrophosphate amidotransferase (1995), J. Biol. Chem., 270, 17394-17399.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and P410W mutant enzyme in Escherichia coli Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
1-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate in wild-type and P410W mutant, competition for the amidotransferase C site Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.031
-
5-phospho-alpha-D-ribose 1-diphosphate P410W mutant enzyme Escherichia coli
0.053
-
5-phospho-alpha-D-ribose 1-diphosphate
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and P410W mutant enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + H2O
-
Escherichia coli L-glutamate + NH3
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.053
-
1-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate P410W mutant enzyme Escherichia coli
0.058
-
1-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate
-
Escherichia coli