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A B 12 -dependent radical SAM enzyme involved in oxetanocin A biosynthesis
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A B 12 -dependent radical SAM enzyme involved in oxetanocin A biosynthesis
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A B 12 -dependent radical SAM enzyme involved in oxetanocin A biosynthesis
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Journal Article
A B 12 -dependent radical SAM enzyme involved in oxetanocin A biosynthesis
2017
Overview
Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA, oxsB, oxrA and oxrB. Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S-adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2'-deoxyadenosine phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2'. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes.
Subject
Adenine - analogs & derivatives
/ Adenosine Monophosphate - metabolism
/ Bacillus megaterium - enzymology
/ Bacillus megaterium - genetics
/ Bacillus megaterium - metabolism
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Deoxyadenine Nucleotides - metabolism
