Literature summary for 1.5.3.6 extracted from

M�hler, H.; Bruhmuller, M.; Decker, K.
Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Identification of the 8 -(N-3-histidyl)-riboflavin-linkage between FAD and apoenzyme (1972), Eur. J. Biochem., 29, 152-155.

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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
FAD	covalently bound to a histidine	Paenarthrobacter nicotinovorans

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Release 2023.1 (January 2023)