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Literature summary for 1.5.3.5 extracted from

  • Brandsch, R.; Hinkkanen, A.E.; Mauch, L.; Nagursky, H.; Decker, K.
    6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase (1987), Eur. J. Biochem., 167, 315-320.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli K12 strain HB101 Paenarthrobacter nicotinovorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-6-hydroxynicotine + H2O + O2 Paenarthrobacter nicotinovorans
-
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nicotinovorans
-
formerly Arthrobacter oxidans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-6-hydroxynicotine + H2O + O2
-
Paenarthrobacter nicotinovorans 1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
?

Cofactor

Cofactor Comment Organism Structure
FAD 1 FAD per subunit, non-covalently bound Paenarthrobacter nicotinovorans
FAD has an adenylate-binding domain Paenarthrobacter nicotinovorans