amidophosphoribosyltransferase
Identifiers
EC no.2.4.2.14
CAS no.9031-82-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme that in humans is encoded by the PPAT (phosphoribosyl pyrophosphate amidotransferase) gene.[1][2]

Function

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ATase is an enzyme that converts α-phosphoribosylpyrophosphate (α-PRPP) into 5-β-phosphoribosylamine. The enzyme uses the ammonia group from the glutamine side-chain. This is the committing step in de novo purine synthesis. It is allosterically inhibited by AMP, GMP, and IMP. 6TGMP (6-thioguanine monophosphate) is a pseudo inhibitor for ATase

ATase is a member of the purine/pyrimidine phosphoribosyltransferase family. This protein is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis.[1]

Interactive pathway map

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Click on genes, proteins and metabolites below to link to respective articles.[§ 1]

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|alt=Fluorouracil (5-FU) Activity edit]]
Fluorouracil (5-FU) Activity edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

References

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  1. ^ a b "Entrez Gene: phosphoribosyl pyrophosphate amidotransferase".
  2. ^ Brayton KA, Chen Z, Zhou G, Nagy PL, Gavalas A, Trent JM, Deaven LL, Dixon JE, Zalkin H (Feb 1994). "Two genes for de novo purine nucleotide synthesis on human chromosome 4 are closely linked and divergently transcribed". The Journal of Biological Chemistry. 269 (7): 5313–21. doi:10.1016/S0021-9258(17)37689-5. PMID 8106516.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.