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Literature summary extracted from

  • Dall-Larsen, T.; Kryvi, H.; Klungsoyr, L.
    Dinitrophenol, dicoumarol and pentachlorophenol as inhibitors and parasite substrates in the ATP phosphoribosyltransferase reaction (1976), Eur. J. Biochem., 66, 443-446.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.17 dicoumarol competitive with respect to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate Escherichia coli
2.4.2.17 dinitrophenol diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate Escherichia coli
2.4.2.17 L-histidine feed-back inhibition Escherichia coli
2.4.2.17 additional information carbonylcyanide m-chlorophenylhydrazone, which is a potent inhibitor of several enzymes with adenine-containing substrates or coenzymes has no effect Escherichia coli
2.4.2.17 Pentachlorophenol competitive to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate Escherichia coli

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 Escherichia coli first step in histidine biosynthesis diphosphate + N-1-(5'-phosphoribosyl)-ATP
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Organism

EC Number Organism UniProt Comment Textmining
2.4.2.17 Escherichia coli
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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
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Escherichia coli 1-(5-phospho-D-ribosyl)-ATP + diphosphate
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r
2.4.2.17 ATP + 5-phospho-alpha-D-ribose 1-diphosphate first step in histidine biosynthesis Escherichia coli diphosphate + N-1-(5'-phosphoribosyl)-ATP
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?