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Xanthine phosphoribosyltransferase

Class of enzymes From Wikipedia, the free encyclopedia

Xanthine phosphoribosyltransferase (EC 2.4.2.22) is an enzyme that catalyzes the phosphorolysis reaction

2D representation of the chemical structure of xanthosine monophosphate .
xanthosine monophosphate
 
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
PPi
 
 
2D representation of the chemical structure of phosphoribosyl pyrophosphate.
phosphoribosyl pyrophosphate
+
 
2D representation of the chemical structure of xanthine.
xanthine
EC no.2.4.2.22
CAS no.9023-10-3
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Xanthine phosphoribosyltransferase
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EC no.2.4.2.22
CAS no.9023-10-3
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The two substrates of this enzyme characterised from Lactobacillus casei are xanthosine monophosphate and pyrophosphate (PPi). Its products are phosphoribosyl pyrophosphate and xanthine.[1]

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.[2]

Structural studies

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

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