Structural and biochemical basis for the firm chemo- and regioselectivity of the nitro-forming N-oxygenase AurF.
نویسندگان
چکیده
Site-directed mutagenesis based on the crystal structure of AurF, a nitro group forming monooxygenase from Streptomyces thioluteus, revealed that AurF variants are capable of selectively transforming guanidyl- and amidinyl-substituted anilines into the corresponding nitro compounds. Our results provide new insights into the biochemical basis of regioselective N-oxygenation.
منابع مشابه
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p-Aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthase starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. AurF is a metalloenzyme, but its native enzymatic activity has not been demonstrated in vitro, and its catalytic mechanism is unclear. In addition, the nature of...
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عنوان ژورنال:
- Chemical communications
دوره 46 41 شماره
صفحات -
تاریخ انتشار 2010