Xanthine phosphoribosyltransferase

In enzymology, a xanthine phosphoribosyltransferase (EC 2.4.2.22) is an enzyme that catalyzes the chemical reaction

XMP + diphosphate 5-phospho-alpha-D-ribose 1-diphosphate + xanthine
xanthine phosphoribosyltransferase
Identifiers
EC number2.4.2.22
CAS number9023-10-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are XMP and diphosphate, whereas its two products are 5-phospho-alpha-D-ribose 1-diphosphate and xanthine.

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is XMP:diphosphate 5-phospho-alpha-D-ribosyltransferase. Other names in common use include Xan phosphoribosyltransferase, xanthosine 5'-phosphate pyrophosphorylase, xanthylate pyrophosphorylase, xanthylic pyrophosphorylase, XMP pyrophosphorylase, 5-phospho-alpha-D-ribose-1-diphosphate:xanthine, phospho-D-ribosyltransferase, 9-(5-phospho-beta-D-ribosyl)xanthine:diphosphate, and 5-phospho-alpha-D-ribosyltransferase. This enzyme participates in purine metabolism.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1A95, 1A96, 1A97, 1A98, 1NUL, and 2FXV.

gollark: And yet it is still uncool and annoying to work with.
gollark: There's a bit of redundancy because there are often multiple different codons which code for the same amino acid.
gollark: Clearly we should just implement Hamming codes or something.
gollark: Hmm, so they indeed might already have some sort of bad ECC available.
gollark: Humans still end up mutating enough to get cancer and annoying stuff like that, sadly.

References
    • Krenitsky TA, Neil SM, Miller RL (1970). "Guanine and xanthine phosphoribosyltransfer activities of Lactobacillus casei and Escherichia coli. Their relationship to hypoxanthine and adenine phosphoribosyltransfer activities". J. Biol. Chem. 245 (10): 2605–11. PMID 4910918.


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