890653-91-5Relevant academic research and scientific papers
Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis
Yokoyama, Kenichi,Kudo, Fumitaka,Kuwahara, Mieko,Inomata, Kousuke,Tamegai, Hideyuki,Eguchi, Tadashi,Kakinuma, Katsumi
, p. 5869 - 5874 (2005)
The doubly functional aminotransferase BtrS in the 2-deoxystreptamine (DOS) biosynthesis, in which two transaminations are involved, was characterized by a genetic as well as a chemical approach with the heterologously expressed enzyme. The gene disruptio
Electrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low-Potential Auxiliary Cluster
Maiocco, Stephanie J.,Grove, Tyler L.,Booker, Squire J.,Elliott, Sean J.
, p. 8664 - 8667 (2015)
The S-adenosylmethionine (AdoMet) radical superfamily of enzymes includes over 113 500 unique members, each of which contains one indispensable iron-sulfur (FeS) cluster that is required to generate a 5′-deoxyadenosyl 5′-radical intermediate during catalysis. Enzymes within several subgroups of the superfamily, however, have been found to contain one or more additional FeS clusters. While these additional clusters are absolutely essential for enzyme activity, their exact roles in the function and/or mechanism of action of many of the enzymes are at best speculative, indicating a need to develop methods to characterize and study these clusters in more detail. Here, BtrN, an AdoMet radical dehydrogenase that catalyzes the two-electron oxidation of 2-deoxy-scyllo-inosamine to amino-dideoxy-scyllo-inosose, an intermediate in the biosynthesis of 2-deoxystreptamine antibiotics, is examined through direct electrochemistry, where the potential of both its AdoMet radical and auxiliary [4Fe-4S] clusters can be measured simultaneously. We find that the AdoMet radical cluster exhibits a midpoint potential of -510 mV, while the auxiliary cluster exhibits a midpoint potential of -765 mV, to our knowledge the lowest [4Fe-4S]2+/+ potential to be determined to date. The impact of AdoMet binding and the pH dependence of catalysis are also quantitatively observed. These data show that direct electrochemical methods can be used to further elucidate the chemistry of the burgeoning AdoMet radical superfamily in the future.
A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
Grove, Tyler L.,Ahlum, Jessica H.,Sharma, Priya,Krebs, Carsten,Booker, Squire J.
scheme or table, p. 3783 - 3785 (2011/03/22)
BtrN catalyzes the two-electron oxidation of the C3 secondary alcohol of 2-deoxy-scyllo-inosamine to the corresponding ketone and is a member of a subclass of radical S-adenosylmethionine (SAM) enzymes called radical SAM (RS) dehydrogenases. Like all RS enzymes, BtrN contains a [4Fe-4S] cluster that delivers an electron to SAM, inducing its cleavage to the common intermediate in RS reactions, the 5′-deoxyadenosyl 5′-radical. In this work, we show that BtrN contains an additional [4Fe-4S] cluster, thought to bind in contact with the substrate to facilitate loss of the second electron in the two-electron oxidation.
Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin
Yokoyama, Kenichi,Numakura, Mario,Kudo, Fumitaka,Ohmori, Daijiro,Eguchi, Tadashi
, p. 15147 - 15155 (2008/09/17)
BtrN encoded in the butirosin biosynthetic gene cluster possesses a CXXXCXXC motif conserved within the radical S-adenosyl methionine (SAM) superfamily. Its gene disruption in the butirosin producer Bacillus circulans caused the interruption of the biosyn
