Abstract
Emodin-1-O-methyltransferase (E-OMT), an enzyme catalysing methylation of emodin and involved in the biosynthesis of (+)-geodin, was purified upto 89 folds by two-step purification with Blue Sepharose and Sepharose 6B column chromatography. The molecular weight of E-OMT was estimated to be 3.4×105, and Km values for emodin and S-adenosylmethionine (SAM) were 3.3×10-7M and 3.1×10-6M, respectively. Substrate specificity of E-OMT was extremely strict, and the enzyme seems to recognize whole the molecule of substrates.
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