88552-21-0Relevant 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.
ISOLATION AND STRUCTURE OF MACOMMELINS, NOVEL METABOLITES OF MACROPHOMA COMMELINAE
Shimizu, Sakae,Sakurai, Ikuo,Yamamoto, Yuzuru
, p. 3781 - 3784 (2007/10/02)
The novel metabolites, named macommelin, macommelin-9-ol, macommelin-8-ol and macommelin-8,9-diol, were isolated from the culture broth of Macrophoma commelinae IFO 9570.The structures were determined to be 5-ethyl-, 5-(2'-hydroxyethyl)-, 5-(1'S-hydroxyethyl)- and 5-(1'S,2'-dihydroxyethyl)-4-methoxy-6-methyl-2H-pyran-2-one, respectively.This fungus also produced rosellisin, an antibiotic α-pyrone. KEYWORDS ---- Macrophoma commelinae IFO 9570; Coelomycetes; fungi; metabolic product; macommelin; macommelin-9-ol; macommelin-8-ol; macommelin-8,9-diol; rosellisin; α-pyrone