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Phosphoribosyl pyrophosphate (PRPP) is a pentose phosphate. It is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, as well as in pyrimidine nucleotide formation. Hence it is a building block for DNA and RNA.
The reaction of PRPP, glutamine, and ammonia forms 5-Phosphoribosyl-1-amine, a precursor to inosinate (IMP), which can ultimately be converted to adenosine triphosphate (ATP) or guanosine triphosphate (GTP). PRPP plays a role in purine salvage pathways by reacting with free purine bases to form adenylate, guanylate, and inosinate.
The formation of 5'-phosphoribosylamine from glutamine and PRPP catalysed by PRPP amino transferase is the regulation point for purine synthesis. The enzyme is an allosteric enzyme, so it can be converted from IMP, GMP and AMP in high concentration binds the enzyme to exerts inhibition while PRPP is in large amount binds to the enzyme which ...
n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is an enzyme encoded in humans by the HPRT1 gene. HGPRT is a transferase that catalyzes conversion of hypoxanthine to inosine monophosphate and guanine to guanosine monophosphate. This ...
231327 Ensembl ENSG00000128059 ENSMUSG00000029246 UniProt Q06203 Q8CIH9 RefSeq (mRNA) NM_002703 NM_172146 RefSeq (protein) NP_002694 NP_742158 Location (UCSC) Chr 4: 56.39 – 56.44 Mb Chr 5: 77.06 – 77.1 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme ...
The generation of reducing equivalents, in the form of NADPH, used in reductive biosynthesis reactions within cells (e.g. fatty acid synthesis). Production of ribose 5-phosphate (R5P), used in the synthesis of nucleotides and nucleic acids. Production of erythrose 4-phosphate (E4P) used in the synthesis of aromatic amino acids.
Orotic acid and PRPP are stabilized in the active site mostly by hydrogen bonding with stabilizing interactions from Lys 26, Phe 34 and Phe 35 to orotic acid, as well as Thr 128, Ala 129, Gly 130, Ala 132, Asp 124, Lys 26 and Lys 73 to PRPP. [14] When Lys 26 is mutated, orotate phosphoribosyltransferase often exhibits reduced activity and ...
Orotate is covalently linked with phosphoribosyl pyrophosphate (PRPP) by orotate phosphoribysol-transferase yielding orotidine monophosphate (OMP). OMP follows with the decarboxylation by orotidylate decarboxylase to form the Uridylate (UMP) ribonucleotide structure. UMP can then be converted to Uridine-5'-trisphosphate (UTP) by two kinases ...