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Insights Into Caerulomycin A Biosynthesis: A Two-Component Monooxygenase CrmH-catalyzed Oxime Formation

Yiguang Zhu, Qingbo Zhang, Sumei Li, Qinheng Lin, Peng Fu, Guangtao Zhang, Haibo Zhang, Rong Shi, Weiming Zhu, Changsheng Zhang

J Am Chem Soc. 2013 Dec 18;135(50):18750-3.

PMID: 24295370

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP21802379 Caerulomycin A Caerulomycin A 21802-37-9 Price
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