EC 2.4.2.17 - ATP phosphoribosyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.2.17

Names

Accepted name:
ATP phosphoribosyltransferase
Other names:
adenosine triphosphate phosphoribosyltransferase
phosphoribosyl ATP synthetase
phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase
phosphoribosyl-ATP pyrophosphorylase
phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase
phosphoribosyladenosine triphosphate pyrophosphorylase
phosphoribosyladenosine triphosphate synthetase
phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase
phosphoribosyl-ATP diphosphorylase
Systematic name:
1-(5-phospho-β-D-ribosyl)-ATP:diphosphate phospho-α-D-ribosyl-transferase

Reaction

Comments:

Involved in histidine biosynthesis.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC01020
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003879
CAS Registry Number: 9031-46-3
UniProtKB/Swiss-Prot: (532) [show] [UniProt]

References

  1. Ames, B.N., Martin, R.G. and Garry, B.J.
    The first step of histidine biosynthesis.
    J. Biol. Chem. 236: 2019-2026 (1961).
  2. Martin, R.G.
    The phosphorolysis of nucleosides by rabbit bone marrow: The nature of feedback inhibition by histidine.
    J. Biol. Chem. 238: 257-268 (1963).
  3. Voll, M.J., Appella, E. and Martin, R.G.
    Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis.
    J. Biol. Chem. 242: 1760-1767 (1967). [PMID: 5337591]

[EC 2.4.2.17 created 1972]