Structural and biochemical basis for the firm chemo- and regioselectivity of the nitro-forming N-oxygenase AurF.
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.
Fries
Alexander
A
Leibniz Institute for Natural Product Research, HKI, Beutenbergstr. 11a, 07745 Jena, Germany.
Winkler
Robert
R
Hertweck
Christian
C
D010129:4-Aminobenzoic Acid / Q000737:chemistry / Q000378:metabolism; D020134:Catalytic Domain; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009584:Nitrogen / Q000378:metabolism; D010084:Oxidation-Reduction; D013237:Stereoisomerism; D013302:Streptomyces / Q000201:enzymology; D013379:Substrate Specificity
D006899:Mixed Function Oxygenases; D009584:Nitrogen; D010129:4-Aminobenzoic Acid