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IUBMB Comments Contains FAD. The enzyme, characterized from the bacterium Arthrobacter sp. Cr-7, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have suggested that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen into the product. The second oxygen atom originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
The enzyme appears in viruses and cellular organisms
Synonyms
5-pyridoxic-acid oxygenase, 5-pyridoxic acid oxygenase,
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5-pyridoxate dioxygenase
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misleading
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5-pyridoxate oxidase
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5-pyridoxic acid oxygenase
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monooxygenase
5-pyridoxic-acid oxygenase
EC 1.14.12.5
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formerly
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5-pyridoxic-acid oxygenase
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5-pyridoxic-acid oxygenase
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3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H+ + O2 = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+
A flavoprotein
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5-pyridoxate,NADPH:oxygen oxidoreductase (ring-opening)
Contains FAD. The enzyme, characterized from the bacterium Arthrobacter sp. Cr-7, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have suggested that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen into the product. The second oxygen atom originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
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3-hydroxy-2-methylpyridine-5-carboxylic acid + NADH
2-[(acetylamino)methylene]succinate + NAD+ + H2O
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
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3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
5-pyridoxic acid + NADPH + O2 + H3O+
2-(acetylaminomethylene)succinate + NADP+ + H2O
additional information
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2,6-dichloroindophenol is no substrate
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3-hydroxy-2-methylpyridine-5-carboxylic acid + NADH
2-[(acetylamino)methylene]succinate + NAD+ + H2O
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poorly utilized substrate analoge
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3-hydroxy-2-methylpyridine-5-carboxylic acid + NADH
2-[(acetylamino)methylene]succinate + NAD+ + H2O
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poorly utilized substrate analoge
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3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
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bacterial vitamin B6 degradation pathway
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3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
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bacterial vitamin B6 degradation pathway
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5-pyridoxic acid + NADPH + O2 + H3O+
2-(acetylaminomethylene)succinate + NADP+ + H2O
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5-pyridoxic acid + NADPH + O2 + H3O+
2-(acetylaminomethylene)succinate + NADP+ + H2O
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5-pyridoxic acid + NADPH + O2 + H3O+
2-(acetylaminomethylene)succinate + NADP+ + H2O
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5-pyridoxic acid + NADPH + O2 + H3O+
2-(acetylaminomethylene)succinate + NADP+ + H2O
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reaction rate 3%
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3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
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bacterial vitamin B6 degradation pathway
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3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
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bacterial vitamin B6 degradation pathway
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FAD
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FAD
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contains 2 mol of FAD+ per mol
FAD
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one FAD per subunit, FMN or riboflavin do not replace FAD as coenzyme
NADH
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NADPH
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6-methylnicotinic acid
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p-chloromercuribenzoate
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0.06
5-pyridoxic acid
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0.2
6-methylnicotinic acid
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6.5 - 8
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broad pH-optimum in phosphate, diphosphate and Tris buffer
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brenda
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brenda
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brenda
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brenda
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brenda
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metabolism
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biodegradation of vitamin B6 in bacteria
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166000
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sedimentation equlibrium
35000
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native enzyme, gel filtration
39200
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native enzyme, sedimentation velocity
40000
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4 * 40000, SDS-PAGE
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tetramer
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4 * 40000, SDS-PAGE
monomer
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1 * 51000, SDS-PAGE
monomer
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1 * 51000, SDS-PAGE
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activity is lost on resolution with acidic ammonium sulfate and can be completely restored with FAD+, but not with FMN
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highly sensitive to sulfhydryl reagents but not to chelating agents and is stabilized by high concentrations of mercaptoethanol and glycerol
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highly sensitive to oxidation
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439054
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-20°C, can be stored up to 1 month with loss about 20% of its activity in a mixture of 50% glycerol and 0.1% 2-mercaptoethanol
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4°C, loses activity rapidly in absence of mercaptoethanol
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Sparrow, L.G.; Ho, P.P.K.; Sundaram, T.K.; Zach, D.; Nyns, E.J.; Snell, E.E.
The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring
J. Biol. Chem.
244
2590-2600
1969
Pseudomonas sp.
brenda
Nelson, M.J.K.; Snell, E.E.
Enzymes of vitamin B6 degradation. Purification and properties of 5-pyridoxic-acid oxygenase from Arthrobacter sp
J. Biol. Chem.
261
15115-15120
1986
Arthrobacter sp., Pseudomonas sp., Arthrobacter sp. Cr7
brenda
Chaiyen, P.
Flavoenzymes catalyzing oxidative aromatic ring-cleavage reactions
Arch. Biochem. Biophys.
493
62-70
2010
Arthrobacter sp.
brenda
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1.14.13.241 5-pyridoxate monooxygenase
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