79214-48-5Relevant articles and documents
Substrate Diversity of Macrophomate Synthase Catalyzing an Unusual Multistep Transformation from 2-Pyrones to Benzoates
Watanabe, Kenji,Mie, Takashi,Ichihara, Akitami,Oikawa, Hideaki,Honma, Mamoru
, p. 530 - 538 (2007/10/03)
Macrophomale synthase, which we have recently purified, catalyzes an unusual multistep transformation from 5-acetyl-4-methoxy-6-methyl-2-pyrone to 4-acetyl-3-methoxy-5-methyl-benzoic acid (macrophomic acid). To investigate the substrate diversity of the enzyme, 40 analogs of 2-pyrone were prepared and their relative efficiency was examined in the enzymatic conversions. The experimental results reveal the structural requirements of the substrates and the rough size of the enzyme active site, and eliminate the ambiguity caused by contamination by other enzymes in the whole-cell experiments.
Studies on Metabolites of Macrophoma commelinae. IV. Substrate Specificity in the Biotransformation of 2-Pyrones to Substituted Benzoic Acids
Sakurai, Ikuo,Miyajima, Hisae,Akiyama, Katsuyoshi,Shimizu, Sakae,Yamamoto, Yuzuru
, p. 2003 - 2011 (2007/10/02)
Substrate specificity in the novel biotransformation from 2-pyrone derivatives to substituted benzoic acids by Macrophoma commelinae (IFO 9570) was investigated by means of feeding experiments with various compounds.Among them, 2-pyrone derivatives substituted by an electron-donating group at C-4, by an electron-withdrawing group at C-5 and by an alkyl group at C-6 were converted to the corresponding benzoic acid derivatives in fairly good yields.The C3-unit precursors and intermediates were examined in stationary or shaking culture.Based on the experimental results obtained, a mechanism for this unique reaction is proposed. macrophoma commelinae IFO 9570; fungi; 2-pyrone; substituted benzoic acid; biotransformation; substrate specificity; aromatic ring formation; macrophomic acid