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Pyrimidine-nucleoside phosphorylase

Class of enzymes From Wikipedia, the free encyclopedia

Pyrimidine-nucleoside phosphorylase (EC 2.4.2.2) is an enzyme that catalyzes several phosphorolysis reactions which convert a pyrimidine nucleoside into the corresponding pyrimidine, by cleavage of the α-D-ribose 1-phosphate sugar unit:[1]

a pyrimidine nucleoside + phosphate (Pi) α-D-ribose 1-phosphate + a pyrimidine base

For example, uridine gives uracil:

 
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
 
 
2D representation of the chemical structure of Q18213356.
ribose 1-phosphate
+
 

The reaction is reversible, so this is also how the pyrimidine nucleosides uridine, cytidine, 2'-deoxyuridine, and thymidine can be made in the bacterium Bacillus stearothermophilus in which the enzyme was characterised.[2][3][4] It has also been described from Enterobacter aerogenes.[5]

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is pyrimidine-nucleoside:phosphate alpha-D-ribosyltransferase. This enzyme is also called Py-NPase.[6]

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes PDB: 1BRW​ and PDB: 2DSJ​.[7]

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