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10.1021/jacs.5b06770

http://scihub22266oqcxt.onion/10.1021/jacs.5b06770
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C4780671!4780671!26266881
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suck abstract from ncbi


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pmid26266881      J+Am+Chem+Soc 2015 ; 137 (34): 10867-9
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  • New Insights into the Conversion of Versicolorin A in the Biosynthesis of Aflatoxin B1 #MMPMID26266881
  • Conradt D; Schätzle MA; Haas J; Townsend CA; Müller M
  • J Am Chem Soc 2015[Sep]; 137 (34): 10867-9 PMID26266881show ga
  • A crucial and enigmatic step in the complex biosynthesis of aflatoxin B1 is the oxidative rearrangement of versicolorin A to demethylsterigmatocystin. This step is thought to proceed by an oxidation?reduction?oxidation sequence, in which the NADPH-dependent oxidoreductase AflM catalyzes the enclosed reduction step. AflM from Aspergillus parasiticus, after heterologous production in E. coli and puriflcation, however, catalyzed the reduction of the hydroquinoid form of the starting compound versicolorin A (25% conversion) to a so far unknown product of aflatoxin biosynthesis. The asymmetric reduction of emodin hydroquinone to (R)-3,8,9,10-tetrahydroxy-6-methyl-3,4-dihydroanthracen-1(2H)-one (up to 82% for AflM) has also been observed in previous studies using MdpC from Aspergillus nidulans (mono-dictyphenone biosynthetic gene cluster). The first (non-enzymatic) reduction of emodin to emodin hydroquinone, for example with sodium dithionite, is obligatory for the enzymatic reduction by AflM or MdpC. These results imply an unprecedented role of AflM in the complex enzymatic network of aflatoxin biosynthesis.
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