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Literature summary for 2.4.2.17 extracted from

  • Tebar, A.R.; Ballesteros, A.O.
    Kinetic properties of ATP phosphoribosyltransferase of Escherichia coli (1976), Mol. Cell. Biochem., 11, 131-136.
    View publication on PubMed
Search for more literature for 2.4.2.17

Inhibitors

Inhibitors Comment Organism Structure
AMP linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation Escherichia coli
ATP inhibits the reaction at high concentrations Escherichia coli
L-histidine feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites 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 diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes Escherichia coli
a
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate double displacement 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
-
 Escherichia coli 1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
 ?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate first step in histidine biosynthesis Escherichia coli diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
 ?