1. Insights into Caerulomycin A Biosynthesis: A Two-Component Monooxygenase CrmH-Catalyzed Oxime Formation.
- Author
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Yiguang Zhu, Qingbo Zhang, Sumei Li, Qinheng Lin, Peng Fu, Guangtao Zhang, Haibo Zhang, Rong Shi, Weiming Zhu, and Changsheng Zhang
- Subjects
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IMMUNOSUPPRESSIVE agents synthesis , *ANTIBIOTICS , *BIPYRIDINE , *OXIMES , *BIOSYNTHESIS , *MONOOXYGENASES , *AMINO acid residues - Abstract
The immunosuppressive agent caerulomycin A features a unique 2,2′-bipyridine core structure and an unusual oxime functionality. Genetic and biochemical evidence confirms that the oxime formation in caerulomycin A biosynthesis is catalyzed by CrmH, a flavin-dependent two-component monooxygenase that is compatible with multiple flavin reductases, from a primary amine via a N-hydroxylamine intermediate. Structure homologue-guided site-directed mutagenesis studies identify four amino acid residues that are essential for CrmH catalysis. This study provides the first biochemical evidence of a two-component monooxygenase that catalyzes oxime formation. [ABSTRACT FROM AUTHOR]
- Published
- 2013
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