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Literature summary for 1.3.98.3 extracted from

  • Yokoyama, K.; Ohmori, D.; Kudo, F.; Eguchi, T.
    Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy (2008), Biochemistry, 47, 8950-8960.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Niallia circulans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.31
-
S-adenosyl-L-methionine apparent value, in the presence of sodium dithionite (10 mM), at room temperature Niallia circulans

Metals/Ions

Metals/Ions Comment Organism Structure
Fe contains 4 irons per polypeptide Niallia circulans

Organism

Organism UniProt Comment Textmining
Niallia circulans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Niallia circulans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine
-
Niallia circulans 3-amino-2,3-dideoxy-scyllo-inosose + CO2 + L-methionine + 5'-deoxyadenosine
-
r

Synonyms

Synonyms Comment Organism
BtrN
-
Niallia circulans
radical S-adenosyl-L-methionine dehydrogenase
-
Niallia circulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.022
-
S-adenosyl-L-methionine apparent value, in the presence of sodium dithionite (10 mM), at room temperature Niallia circulans

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center contains one [4Fe-4S]+ cluster per monomer Niallia circulans