Involved in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family. The enzyme from Bacillus circulans was shown to be a radical S-adenosyl-L-methionine (SAM) enzyme. cf. EC 1.1.1.329, 2-deoxy-scyllo-inosamine dehydrogenase.
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The enzyme appears in viruses and cellular organisms
Involved in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family. The enzyme from Bacillus circulans was shown to be a radical S-adenosyl-L-methionine (SAM) enzyme. cf. EC 1.1.1.329, 2-deoxy-scyllo-inosamine dehydrogenase.
when AdoMet and 2-deoxy-scyllo-inosamine are bound, reduction of the active site cluster in a pH dependent fashion allows for reductive cleavage of AdoMet, generating a 5'-deoxyadenosine radical,which can then abstract a hydrogen atom from the 2-deoxy-scyllo-inosamine substrate forming a 2-deoxy-scyllo-inosamine radical. The 2-deoxy-scyllo-inosamine radical has an estimated potential of -1.6 V, indicating that it could easily reduce either the auxiliary cluster or the AdoMet radical cluster itself
enzyme catalyzes the oxidation of 2-deoxy-scyllo-inosamine under strictly anaerobic conditions along with consumption of an equimolar amount of S-adenosyl-L-methionine to produce 5-deoxyadenosine, methionine, and 3-amino-2,3-dideoxy-scylloinososeReaction follows the ordered Bi Ter mechanism and S-adenosyl-L-methionine is the first substrate and 2-deoxy-scyllo-inosamine is the second. The hydrogen atom at C-3 of 2-deoxy-scyllo-inosamine is directly transferred to 5-deoxyadenosine to give the radical intermediate of 2-deoxy-scyllo-inosamine in a reversible hydrogen abstraction step
radical S-adenosyl-L-methionine enzyme. Ketone formation is the rate-determining step in this reaction. Reaction involves formation of a 2-deoxy-scyllo-inosamine radical which can easily be converted to a highly reductive ketyl radical by deprotonation through proton-coupled electron transfer
BtrNcontains a [4Fe-4S] cluster that delivers an electron to SAM, inducing its cleavage to the common intermediate in radical SAM reactions, the 5'-deoxyadenosyl 5'-radical. 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
the potential of both the AdoMet [4Fe-4S] radical and auxiliary clusters can be measured simultaneously. The AdoMet [4Fe-4S] radical cluster exhibits a midpoint potential of -510 mV, while the auxiliary cluster exhibits a midpoint potential of -765 mV
BtrNcontains a [4Fe-4S] cluster that delivers an electron to SAM, inducing its cleavage to the common intermediate in radical SAM reactions, the 5'-deoxyadenosyl 5'-radical. 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
gene disruption causes the interruption of the biosynthetic pathway between 2-deoxy-scyllo-inosamine and 2-deoxystreptamine. In vitro assay of the overexpressed enzyme reveals that the enzyme catalyzes the oxidation of 2-deoxy-scyllo-inosamine under strictly anaerobic conditions along with consumption of an equimolar amount of S-adenosyl-L-methionine to produce 5-deoxyadenosine, methionine, and 3-amino-2,3-dideoxy-scyllo-inosose
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of electron paramagnetic resonance signals for free enzyme, the enzyme-S-adenosyl-L-methionine complex, and a rhombic signal presumably derived from the enzyme-S-adenosyl-L-methionine-substrate ternary complex show close interaction of both S-adenosyl-L-methione and 2-deoxy-scyllo-inosamine with the [4Fe-4S] cluster
in complex with AdoMet and substrate, to 1.56 A resolution. Structure displays a modification to the core AdoMet radical fold, instead of the canonical (beta/alpha)6 architecture, BtrN displays a (beta5/alpha4) motif. An auxiliary [4Fe-4S] cluster in BtrN, thought to bind substrate, is instead implicated in substrate-radical oxidation
Maiocco, S.J.; Grove, T.L.; Booker, S.J.; Elliott, S.J.
Electrochemical resolution of the [4Fe-4S] centers of the AdoMet radical enzyme BtrN: evidence of proton coupling and an unusual, low-potential auxiliary cluster
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1.1.99.38 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)
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