Characterization of purine hydroxylase I from Aspergillus nidulans.
Purine hydroxylase I from Aspergillus nidulans was purified 850-fold. The purified preparations exhibited the spectral and catalytic properties, including broad specificity for oxidizing and reducing substrates, typical of molybdenum/flavin/iron-sulphur-containing hydroxylases (oxotransferases).
Mehra
R K
RK
Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Ireland.
Coughlan
M P
MP
D001233:Aspergillus nidulans / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007658:Ketone Oxidoreductases / Q000302:isolation & purification*; D009243:NAD / Q000378:metabolism; D013379:Substrate Specificity; D014968:Xanthine Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism
D009243:NAD; D014968:Xanthine Dehydrogenase; D007658:Ketone Oxidoreductases