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Literature summary 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

Inhibitors

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.17 ATP + 5-phospho-alpha-D-ribose 1-diphosphate Acinetobacter baumannii
-
 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.17 Acinetobacter baumannii
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.4.2.17 ATPPRT
-
 Acinetobacter baumannii

General Information

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