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Literature summary for 1.5.3.6 extracted from

  • Stoltz, M.; Henninger, H.P.; Brandsch, R.
    The design of an alternative, covalently flavinylated 6-hydroxy-D-nicotine oxidase by replacing the FAD-binding histidine by cysteine and reconstitution of the holoenzyme with 8-(methylsulfonyl)FAD (1996), FEBS Lett., 386, 194-196.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 Paenarthrobacter nicotinovorans

Protein Variants

Protein Variants Comment Organism
H71C 80% activity of wild-type Paenarthrobacter nicotinovorans

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nicotinovorans
-
-
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
FAD bound as 8-(N-acetylcysteinyl)FAD 80% activity of the wild type enzyme, H71C mutant Paenarthrobacter nicotinovorans
FAD formation of the bond to FAD proceeds autocatalytically Paenarthrobacter nicotinovorans