Aryl monooxygenase: a detoxifying enzyme from Candida pulcherrima MCMY2.
Characterization of partially purified aryl monooxygenase (1:14:14:1) from Candida pulcherrima MCMY2 was achieved using standard purification protocol. The molecular weight of the enzyme was 110 kDa and contained 3 subunits with pI 5.7, 7.4 and 7.6. The activity seemed to be related with pulcherrimin. The optimum pH and temperature for enzyme activity were 6.8 and 30 degrees C respectively. Activity was not substrate specific and Fe3+ FAD and NADH+ enhanced the activity substantially.
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Division of Microbial Sciences, Agharkar Research Institute, Pune, India.
D001189:Aryl Hydrocarbon Hydroxylases / Q000302:isolation & purification* / Q000378:metabolism; D002175:Candida / Q000201:enzymology*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005290:Ferric Compounds / Q000494:pharmacology; D005182:Flavin-Adenine Dinucleotide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D011487:Protein Conformation; D013379:Substrate Specificity; D013696:Temperature
D005290:Ferric Compounds; D005182:Flavin-Adenine Dinucleotide; D003577:Cytochrome P-450 Enzyme System; D001189:Aryl Hydrocarbon Hydroxylases