Literature summary for 2.4.2.17 extracted from

Lohkamp, B.; McDermott, G.; Campbell, S.A.; Coggins, J.R.; Lapthorn, A.J.
The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition (2004), J. Mol. Biol., 336, 131-144.

Search for more literature for 2.4.2.17

Cloned(Commentary)

Cloned (Comment)	Organism
expression of selenomethionine-labeled enzyme in strain B834(DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant selenomethionine-labeled enzyme in complex with inhibitor AMP or with product 1-(5-phospho-D-ribosyl)-ATP, X-ray diffraction enzyme-inhibitor complex structure determination and analysis at 2.7 A resolution, X-ray diffraction enzyme-product complex structure determination and analysis at 2.9 A resolution, modeling	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
AMP	binding structure and inhibition mode	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required for substrate binding	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + 5-phospho-alpha-D-ribose 1-diphosphate	Escherichia coli	first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway	1-(5-phospho-D-ribosyl)-ATP + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P60757	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant selenomethionine-labeled enzyme from strain B834(DE3)	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate	substrate binding sites, e.g. Cys104, Asn75, Ser154, Glu156, and Val155, reaction mechanism	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + 5-phospho-alpha-D-ribose 1-diphosphate	first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway	Escherichia coli	1-(5-phospho-D-ribosyl)-ATP + diphosphate	-	?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate	-	Escherichia coli	1-(5-phospho-D-ribosyl)-ATP + diphosphate	-	?

Subunits

Subunits	Comment	Organism
additional information	quarternary structure	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ATP-phosphoribosyltransferase	-	Escherichia coli
ATP-PRT	-	Escherichia coli

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)