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Literature summary for 2.4.2.17 extracted from

  • Pedreno, S.; Pisco, J.P.; Larrouy-Maumus, G.; Kelly, G.; de Carvalho, L.P.
    Mechanism of feedback allosteric inhibition of ATP phosphoribosyltransferase (2012), Biochemistry, 51, 8027-8038.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
codon adapted to Escherichia coli, synthetically prepared, His-tagged protein expressed in Escherichia coli BL21(DE3)pLysS Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Mycobacterium tuberculosis
L-histidine allosteric inhibitor, inhibition dependent on pH, uncompetitive versus ATP, noncompetitive versus 5-phospho-alpha-D-ribosyl diphosphate Mycobacterium tuberculosis
Mg2+ at high concentrations, Ki = 23 mM Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.049
-
5-phospho-alpha-D-ribose 1-diphosphate pH 8.5, 25°C Mycobacterium tuberculosis
0.263
-
ATP pH 8.5, 25°C Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
K+
-
Mycobacterium tuberculosis
Mg2+ Kact = 1.9 mM; Ki = 23 mM Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
180000
-
gel filtration Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis H37Rv
-
-
-

Purification (Commentary)

Purification (Comment) Organism
immobilized metal ion affinity chromatography (Ni2+) Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis 1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis H37Rv 1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
-
r

Subunits

Subunits Comment Organism
homohexamer 6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ATP phosphoribosyltransferase
-
Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.004
-
L-histidine uncompetitive versus ATP, pH 8.0, 25°C Mycobacterium tuberculosis
0.0079
-
L-histidine uncompetitive versus ATP, pH 8.25, 25°C Mycobacterium tuberculosis
0.0235
-
L-histidine Kii-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25°C Mycobacterium tuberculosis
0.0257
-
L-histidine Kis-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25°C Mycobacterium tuberculosis
0.0269
-
L-histidine uncompetitive versus ATP, pH 8.75, 25°C Mycobacterium tuberculosis
0.0279
-
L-histidine uncompetitive versus ATP, pH 8.5, 25°C Mycobacterium tuberculosis
0.0504
-
L-histidine uncompetitive versus ATP, pH 9.0, 25°C Mycobacterium tuberculosis
0.1094
-
L-histidine uncompetitive versus ATP, pH 9.25, 25°C Mycobacterium tuberculosis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.033
-
pH 8.5, 25°C Mycobacterium tuberculosis L-histidine