Aryl monooxygenase: a detoxifying enzyme from Candida pulcherrima MCMY2.
Indian J Biochem Biophys
;
1996 Dec; 33(6): 523-6
Article
in English
| IMSEAR
| ID: sea-26522
ABSTRACT
Characterization of partially purified aryl monooxygenase (114141) 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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Protein Conformation
/
Substrate Specificity
/
Temperature
/
Candida
/
Aryl Hydrocarbon Hydroxylases
/
Ferric Compounds
/
Cytochrome P-450 Enzyme System
/
Enzyme Activation
/
Flavin-Adenine Dinucleotide
/
Hydrogen-Ion Concentration
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1996
Type:
Article
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