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.

Search for more literature for 2.4.2.17

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2026.1 (March 2026)