| Literature DB >> 24295370 |
Yiguang Zhu1, Qingbo Zhang, Sumei Li, Qinheng Lin, Peng Fu, Guangtao Zhang, Haibo Zhang, Rong Shi, Weiming Zhu, Changsheng Zhang.
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.Entities:
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Year: 2013 PMID： 24295370 DOI： 10.1021/ja410513g
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419