| amidolysis, amido+, amidino+ | |
| amidorphin, amidorphin, amiloride |
| amidophosphoribosyltransferase | |||||||
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| Identifiers | |||||||
| EC number | 2.4.2.14 | ||||||
| CAS number | 9031-82-7 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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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]
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Contents
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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.
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]
Click on genes, proteins and metabolites below to link to respective articles. [3]
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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