Literature summary for 1.5.3.6 extracted from

Mauch, L.; Bichler, V.; Brandsch, R.
Lysine can replace arginine 67 in the mediation of covalent attachment of FAD to histidine 71 of 6-hydroxy-D-nicotine oxidase (1990), J. Biol. Chem., 265, 12761-12762.

Search for more literature for 1.5.3.6

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
R67A	no enzyme activity, no flavinylation	Paenarthrobacter nicotinovorans
R67K	3% activity of wild-type, better flavinylation rate than wild type enzyme	Paenarthrobacter nicotinovorans
S68A	80% activity of wild-type, flavinylation	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	-	formerly Arthrobacter oxidans	-

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

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Release 2023.1 (January 2023)