Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 50, Pages 18750-18753Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja410513g
Keywords
-
Categories
Funding
- MOST [2010CB833805]
- NSFC [31125001, 31070045]
- CAS [KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available