Structural highlights
Function
XAPA_ECOLI The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. This protein can degrade all purine nucleosides including xanthosine, inosine and guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine arabinoside. Has a preference for the neutral over the monoanionic form of xanthosine.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Buxton RS, Hammer-Jespersen K, Valentin-Hansen P. A second purine nucleoside phosphorylase in Escherichia coli K-12. I. Xanthosine phosphorylase regulatory mutants isolated as secondary-site revertants of a deoD mutant. Mol Gen Genet. 1980;179(2):331-40. PMID:7007808
- ↑ Hammer-Jespersen K, Buxton RS, Hansen TD. A second purine nucleoside phosphorylase in Escherichia coli K-12. II. Properties of xanthosine phosphorylase and its induction by xanthosine. Mol Gen Genet. 1980;179(2):341-8. PMID:7007809
- ↑ Koszalka GW, Vanhooke J, Short SA, Hall WW. Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12. J Bacteriol. 1988 Aug;170(8):3493-8. PMID:3042752
- ↑ Dandanell G, Szczepanowski RH, Kierdaszuk B, Shugar D, Bochtler M. Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene. J Mol Biol. 2005 Apr 22;348(1):113-25. PMID:15808857 doi:http://dx.doi.org/10.1016/j.jmb.2005.02.019
