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Literature summary for 2.4.2.14 extracted from

  • Zalkin, H.
    Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes (1983), Adv. Enzyme Regul., 21, 225-237.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli
expression in Escherichia coli Bacillus subtilis

General Stability

General Stability Organism
AMP or GMP stabilizes dimeric enzyme form Bacillus subtilis
GDP stabilizes tetrameric enzyme form Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.072
-
5-phospho-alpha-D-ribose 1-diphosphate
-
Bacillus subtilis
4.3
-
L-glutamine
-
Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe enzyme contains a diamagnetic [4Fe-4S] cluster essential for activity Bacillus subtilis
additional information
-
Gallus gallus
additional information non-heme iron is not present in significant amounts Escherichia coli
additional information probably diamagnetic Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
-
Gallus gallus
50000
-
2-4 * 50000, SDS-PAGE Bacillus subtilis
56395
-
3-4 * 56395, calculated from nucleotide sequence Escherichia coli
57000
-
3-4 * 57000, SDS-PAGE Escherichia coli
194000
-
sedimentation equilibrium centrifugation Escherichia coli
224000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-
Gallus gallus
-
-
-

Oxidation Stability

Oxidation Stability Organism
in vitro O2 oxidizes iron in the Fe-S cluster to the high spin ferric state and sulfur to a mixtur of S in thiocystine residues plus other unidentified products Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O mechanism of glutamine amide transfer Bacillus subtilis
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O mechanism of glutamine amide transfer Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.043
-
-
Bacillus subtilis
17.2
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
Gallus gallus 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
Escherichia coli 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O reaction at 70% the rate of aminotransferase activity Bacillus subtilis 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
Gallus gallus 5-phospho-beta-D-ribosylamine + diphosphate
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O no activity with NH4+ Bacillus subtilis 5-phospho-beta-D-ribosylamine + diphosphate
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O no activity with NH4+ Escherichia coli 5-phospho-beta-D-ribosylamine + diphosphate
-
?

Subunits

Subunits Comment Organism
?
-
Gallus gallus
? 2-4 * 50000, SDS-PAGE Bacillus subtilis
? 3-4 * 56395, calculated from nucleotide sequence Escherichia coli
? 3-4 * 57000, SDS-PAGE Escherichia coli