ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathway.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 7 citations in OpenAlex.
- How a cofactor-free protein environment lowers the barrier to OThe Journal of biological chemistry · 2019Article
- Monooxygenase Substrates Mimic Flavin to Catalyze Cofactorless Oxygenations.The Journal of biological chemistry · 2016Article
- Divergent evolution of an atypical S-adenosyl-l-methionine-dependent monooxygenase involved in anthracycline biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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4 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
12-deoxy-nogalonic acid oxygenase (SnoaB) catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid, which is one of the steps in the biosynthesis of the polyketide nogalamycin in Streptomyces nogalater. SnoaB belongs to a family of small cofactor-free oxygenases which carry out oxygenation reactions without the aid of any prosthetic group, cofactor or metal ion. Recombinant SnoaB was crystallized in space group P2(1)2(1)2, with unit-cell parameters a = 58.8, b = 114.1, c = 49.5 A, and these crystals diffracted to 2.4 A resolution. Recombinant SnoaB does not contain any methionine residues and three double mutants were designed and produced for the preparation of selenomethionine-substituted samples. The selenomethionine-substituted mutant F40M/L89M crystallized in the same space group as the native enzyme.
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