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Literature summary for 1.1.99.38 extracted from

  • 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 (2015), J. Am. Chem. Soc., 137, 8664-8667.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Niallia circulans Q8G907
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine
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Niallia circulans 3-amino-2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + L-methionine 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 ?

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center 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 Niallia circulans