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Literature summary for 2.4.2.17 extracted from

  • Read, B.J.; Fisher, G.; Wissett, O.L.R.; Machado, T.F.G.; Nicholson, J.; Mitchell, J.B.O.; da Silva, R.G.
    Allosteric inhibition of Acinetobacter baumannii ATP phosphoribosyltransferase by protein dipeptide and protein protein interactions (2022), ACS Infect. Dis., 8, 197-209.
    View publication on PubMed
Search for more literature for 2.4.2.17

Inhibitors

Inhibitors Comment Organism Structure
L-histidine noncompetitive inhibition, subunit HisZ activates subunit HisGS and mediates allosteric inhibition by histidine Acinetobacter baumannii

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 Acinetobacter baumannii
-
 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Acinetobacter baumannii 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 ?

Subunits

Subunits Comment Organism
heterooctamer catalytic (HisGS) and regulatory (HisZ) subunits assemble in a heterooctamer Acinetobacter baumannii

Synonyms

Synonyms Comment Organism
ATPPRT
-
 Acinetobacter baumannii

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the first step of histidine biosynthesis Acinetobacter baumannii
physiological function subunit HisGS is necessary for the bacterium to persist in the lung during pneumonia Acinetobacter baumannii