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Literature summary for 1.5.3.6 extracted from

  • Stoltz, M.; Brandsch, R.
    The conformational change induced by FAD in covalently flavinylated 6-hydroxy-D-nicotine oxidase does not require (8alpha)FAD(N3)histidyl bond formation (1998), J. Biochem., 123, 445-449.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli S30 wild type and mutants Paenarthrobacter nicotinovorans

Protein Variants

Protein Variants Comment Organism
H71C only residual enzyme activity Paenarthrobacter nicotinovorans
P73A unable to bind FAD 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 FAD is bound via an (8alpha)-isoalloxazine-(N3)histidyl linkage Paenarthrobacter nicotinovorans