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Literature summary for 1.17.1.4 extracted from

  • Srivastava, M.; Mallard, C.; Barke, T.; Hancock, L.E.; Self, W.T.
    A selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production (2011), J. Bacteriol., 193, 1643-1652.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information isolation of selD and xdh in-frame deletion mutants with null phenotype for biofilm formation. The wild-type strain produces significant levels of superoxide, whereas the selD and xdh mutants do not exhibit superoxide production, overview Enterococcus faecalis

Metals/Ions

Metals/Ions Comment Organism Structure
selenium dependent on, selenium is required in a labile form Enterococcus faecalis

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis
-
 gene xdh
-

Synonyms

Synonyms Comment Organism
XDH
-
 Enterococcus faecalis

General Information

General Information Comment Organism
metabolism xanthine dehydrogenase activity correlates with the presence of this labile selenoprotein complex and is absent in a selD, encoding selenophosphate synthetase, or an xdh mutant, overview. Peroxide levels are not increased in either the selD or the xdh mutant upon addition of selenite Enterococcus faecalis
additional information biofilm formation is stimulated in the presence of uric acid, Se, and Mo and inhibited by auranofin or tungstate Enterococcus faecalis
physiological function xanthine dehydrogenase is necessary for extracellular superoxide and hydrogen peroxide production by the organism. The selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production Enterococcus faecalis