Ribose-phosphate diphosphokinase

Ribose-phosphate diphosphokinase
Phosphoribosyl pyrophosphate synthase 1, hexamer, Human
Identifiers
EC no.2.7.6.1
CAS no.9031-46-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
phosphoribosyl pyrophosphate synthetase 1
Identifiers
SymbolPRPS1
NCBI gene5631
HGNC9462
OMIM311850
RefSeqNM_002764
UniProtP60891
Other data
EC number2.7.6.1
LocusChr. X q21-q27
Search for
StructuresSwiss-model
DomainsInterPro
phosphoribosyl pyrophosphate synthetase 2
Identifiers
SymbolPRPS2
NCBI gene5634
HGNC9465
OMIM311860
RefSeqNM_002765
UniProtP11908
Other data
EC number2.7.6.1
LocusChr. X pter-q21
Search for
StructuresSwiss-model
DomainsInterPro

Ribose-phosphate diphosphokinase (or phosphoribosyl pyrophosphate synthetase or ribose-phosphate pyrophosphokinase) is an enzyme that converts ribose 5-phosphate into phosphoribosyl pyrophosphate (PRPP).[1][2] It is classified under EC 2.7.6.1.

The enzyme is involved in the synthesis of nucleotides (purines and pyrimidines), cofactors NAD and NADP, and amino acids histidine and tryptophan,[1][2][3] linking these biosynthetic processes to the pentose phosphate pathway, from which the substrate ribose 5-phosphate is derived. Ribose 5-phosphate is produced by the HMP Shunt Pathway from Glucose-6-Phosphate. The product phosphoribosyl pyrophosphate acts as an essential component of the purine salvage pathway and the de novo synthesis of purines. Dysfunction of the enzyme would thereby undermine purine metabolism. Ribose-phosphate pyrophosphokinase exists in bacteria, plants, and animals, and there are three isoforms of human ribose-phosphate pyrophosphokinase.[2] In humans, the genes encoding the enzyme are located on the X chromosome.[2]

  1. ^ a b Visentin LP, Hasnain S, Gallin W (July 1977). "Ribosomal protein S1/S1A in bacteria". FEBS Lett. 79 (2): 258–63. Bibcode:1977FEBSL..79..258V. doi:10.1016/0014-5793(77)80799-0. PMID 330231. S2CID 38926849.
  2. ^ a b c d Li S, Lu Y, Peng B, Ding J (January 2007). "Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site". Biochem. J. 401 (1): 39–47. doi:10.1042/BJ20061066. PMC 1698673. PMID 16939420.
  3. ^ Tang W, Li X, Zhu Z, Tong S, Li X, Zhang X, Teng M, Niu L (May 2006). "Expression, purification, crystallization and preliminary X-ray diffraction analysis of human phosphoribosyl pyrophosphate synthetase 1 (PRS1)". Acta Crystallographica Section F. 62 (Pt 5): 432–4. doi:10.1107/S1744309106009067. PMC 2219982. PMID 16682768.