Uridine phosphorylase
Class of enzymes
From Wikipedia, the free encyclopedia
Uridine phosphorylase (EC 2.4.2.3) is an enzyme that catalyzes a phosphorolysis reaction which converts the pyrimidine nucleotide, uridine, into uracil, by cleavage of the α-D-ribose 1-phosphate sugar unit:
This is part of a salvage pathway that allows the organisms in which the enzyme occurs to recycle the nucleotide into its component parts.[1][2][3] The enzyme has been characterised in Escherichia coli and humans.[4][5]
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is uridine:phosphate alpha-D-ribosyltransferase. Other names in common use include pyrimidine phosphorylase, UrdPase, UPH, and UPase.[6]
Structural studies
As of late 2007, 27 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1K3F, PDB: 1LX7, PDB: 1RXC, PDB: 1RXS, PDB: 1RXU, PDB: 1RXY, PDB: 1RYZ, PDB: 1SJ9, PDB: 1SQ6, PDB: 1T0U, PDB: 1TGV, PDB: 1TGY, PDB: 1U1C, PDB: 1U1D, PDB: 1U1E, PDB: 1U1F, PDB: 1U1G, PDB: 1Y1Q, PDB: 1Y1R, PDB: 1Y1S, PDB: 1Y1T, PDB: 1ZL2, PDB: 2HN9, PDB: 2HRD, PDB: 2HSW, PDB: 2HWU, and PDB: 2I8A.
