100507-74-2Relevant articles and documents
Active site mutagenesis of the putative Diels-Alderase macrophomate synthase
Serafimov, Joerg M.,Lehmann, Hans Christian,Oikawa, Hideaki,Hilvert, Donald
, p. 1701 - 1703 (2007)
Although the macrophomate synthase active site is rich in potential functional groups, site-directed mutagenesis shows that only three residues are absolutely required for catalysis of oxaloacetate decarboxylation and trapping of the resulting enolate wit
Macrophomate synthase: Unusual enzyme catalyzing multiple reactions from pyrones to benzoates
Oikawa, Hideaki,Watanabe, Kenji,Yagi, Kenji,Ohashi, Satoshi,Mie, Takashi,Ichihara, Akitami,Honma, Mamoru
, p. 6983 - 6986 (2007/10/03)
Macrophomate synthase which catalyzes unusual multiple reactions from 2-pyrone (3) to macrophomic acid (1) has been purified in a homogenous state. The macrophomate synthase is a dimeric enzyme which requires Mg2+ as a co-factor and whose molec
NOVEL BIOTRANSFORMATION OF A 2-PYRONE TO A SUBSTITUTED BENZOIC ACID
Sakurai, Ikuo,Suzuki, Harumi,Shimizu, Sakae,Yamamoto, Yuzuru
, p. 5141 - 5143 (2007/10/02)
It was found that Macrophoma commelinae (IFO 9570) has an ability to transform 5-acetyl-4-methoxy-6-methyl-2-pyrone (1) to 4-acetyl-3-methoxy-5-methylbenzoic acid (2).This biotransformation was investigated using 13C- and 14C-labeled compounds.It is likely that 2 is formed by condensation of the added 2-pyrone and a catabolic pyruvate.KEYWORDS-Macrophoma commelinae; fungus; 2-pyrone; substituted benzoic acid; pyruvate; aromic ring formation
