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Literature summary for 2.4.2.14 extracted from

  • Kim, J.H.; Krahn, J.M.; Tomchick, D.R.; Smith, J.L.; Zalkin, H.
    Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site (1996), J. Biol. Chem., 271, 15549-15557.
    View publication on PubMed
Search for more literature for 2.4.2.14

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of 6-diazo-5-oxonorleucine inactivated enzyme at 2.3 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
R26H extremely labile enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic constants of Arg73 and Tyr74 mutants for basal and total glutaminase activity Escherichia coli
0.64
-
 L-glutamine N101G mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity Escherichia coli
1.42
-
 L-glutamine N101D mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity Escherichia coli
1.72
-
 L-glutamine 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutamine hydrolysis Escherichia coli
1.72
-
 L-glutamine wild-type enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity Escherichia coli
2.1
-
 L-glutamine
-
 Escherichia coli
2.43
-
 L-glutamine G102A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity Escherichia coli
6.03
-
 L-glutamine N101G mutant enzyme, aminotransferase activity Escherichia coli
6.08
-
 L-glutamine D127A mutant enzyme, aminotransferase activity Escherichia coli
7.31
-
 L-glutamine R73L mutant enzyme, aminotransferase activity Escherichia coli
7.34
-
 NH3
-
 Escherichia coli
7.34
-
 L-glutamine wild-type enzyme, aminotransferase activity Escherichia coli
7.67
-
 L-glutamine G102A mutant enzyme, aminotransferase activity Escherichia coli
9.17
-
 L-glutamine N101D mutant enzyme, aminotransferase activity Escherichia coli
9.76
-
 L-glutamine R73H mutant enzyme, aminotransferase activity Escherichia coli
101
-
 L-glutamine R73H mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity Escherichia coli
110
-
 L-glutamine R73L mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity Escherichia coli
193
-
 glutamine 5-phospho-alpha-D-ribose 1-diphosphate-independent glutamine hydrolysis Escherichia coli
236
-
 L-glutamine D127A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O binding of 5-phospho-alpha-D-ribose 1-diphosphate activates the enzyme by a structural change that lowers the Km for glutamine 100fold and couples glutamine hydrolysis to synthesis of 5-phospho-beta-D-ribosylamine Escherichia coli
a

Substrates and Products (Substrate)

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