Partial purification and some properties of emodin-O-methyltransferase from (+)-geodin producing strain of Aspergillus terreus

Abstract

Emodin-l-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 × 10−7 M and 3.1 × 10−6 M, respectively. Substrate specificity of E-OMT was extremely strict, and the enzyme seems to recognize whole the molecule of substrates. © 1982, The Pharmaceutical Society of Japan. All rights reserved.