Methyl transferase, a polyketide biosynthetic enzyme from Dreschlera monceras: purification and properties
Abstract
Methyl transferase, a polyketide biosynthetic enzyme in monocerin biosynthesis was isolated and purified from Dreschlera monoceras. The enzyme was purified to near homogeneity with 11.1% recovery, using ammonium sulphate fractionation followed by ultra filtration, SP Sepharose chromatography and gel filtration chromatography. The molecular mass of the purified enzyme as determined by elution through Superdex TM gel filtration chromatography was found to ~ 165kDa. SDS-PAGE of the purified enzyme showed a single band at ~55kDa indicating that possibly enzyme could be a trimer of 3 subunits. The enzyme showed optimum pH at 7.5-7.7, whereas optimum assay temperature was 35-37°C. Enzyme was stable up to 45°C and above this temperature enzyme activity slowly declined and inactivated around 70°C. Apparent Km of the enzyme was found to be ~ 0.083mM.
Keywords: methyl transferase; monocerin biosynthesis; polyketides; D. monoceras.
DOI: 10.4038/josuk.v3i0.2734
J. Sci. Univ. Kelaniya 3 (2007) : 1-16
© 2011 MKB Weerasooriya, J Crosby, published by Faculty of Science of the University of Kelaniya, Sri Lanka
This work is licensed under the Creative Commons License.