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EC Tree
IUBMB Comments Contains FAD. The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have shown that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen. The second oxygen atom that is incorporated into the product originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
mhpco, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase,
mlr6788 ,
more
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2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase
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2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
3-hydroxy-2-methylpyridine carboxylate dioxygenase
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3-hydroxy-2-methylpyridinecarboxylate dioxygenase
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misleading
methylhydroxypyridine carboxylate dioxygenase
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methylhydroxypyridinecarboxylate oxidase
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2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase
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2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase
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2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase
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2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase
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2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
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2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
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2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
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MHPCO
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mlr6788
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locus name
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3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
reaction proceeds in a concerted fashion via a ternary complex of oxygenase, NADH and 3-hydroxy-2-methylpyridine-5-carboxylate
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3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
ordered mechanism in which 3-hydroxy-2-methylpyridine-5-carboxylate binds first, followed by NADH. The first product NAD+ is then released, followed by oxygen binding and finally release of the oxygenated and reduced cleavage product 2-(acetamidomethylene)succinate
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3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
the enzyme catalyzes both a classical hydroxylation and a subsequent unique hydrolysis of the hydroxylated substrate to yield the acyclic product
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3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
the binding proceeds in two steps: an enzyme-substrate complex initially formed is followed by a ligand-induced isomerization
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3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
oxygenation reaction occurs via an electrophilic aromatic substitution mechanism
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3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylidene)succinate + NAD(P)+
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3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (ring-opening)
Contains FAD. The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6). Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have shown that it is a monooxygenase, incorporating only one oxygen atom from molecular oxygen. The second oxygen atom that is incorporated into the product 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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2-methyl-3-hydroxypyridine-5-carboxylic acid + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2
2-(acetamidomethylene)succinate + NAD(P)+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADPH + H+ + O2
2-(acetamidomethylene)succinate + NADP+
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?
5-hydroxynicotinate + NAD(P)H + H+ + O2
? + NAD(P)+
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-
-
?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
5-hydroxynicotinic acid + NADH + O2
?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5-pyridoxic acid + NADH + O2
?
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-
-
?
5-pyridoxic acid + NADH + O2 + H+
2-(acetamidomethylene)-beta-hydroxymethyl succinate + NAD+
5% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
N-methyl-5-hydroxynicotinic acid + NADH + O2
?
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-
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?
additional information
?
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3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
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-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+ + H2O
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD(P)+
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the nitrogen atom of the 3-hydroxy-2-methylpyridine-5-carboxylate is invariably protonated during the catalytic reaction
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
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inducible enzyme opens the pyridine ring during the metabolic degradation of vitamin B6
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
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enzyme is involved in degradation of vitamin B6
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
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?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
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?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
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?
5-hydroxynicotinic acid + NADH + H+ + O2
alpha-(N-formylaminomethylene)succinic acid + NAD+ + H2O
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?
5-hydroxynicotinic acid + NADH + O2
?
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?
5-hydroxynicotinic acid + NADH + O2
?
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?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
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?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
about 100% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
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?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
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?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
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?
5-pyridoxic acid + NADH + H+ + O2
alpha-(N-acetylaminomethylene)-beta-hydroxymethyl succinic acid + NAD+ + H2O
5% activity compared to 3-hydroxy-2-methylpyridine-5-carboxylate
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?
additional information
?
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also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
additional information
?
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also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
additional information
?
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also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
additional information
?
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also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
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2-methyl-3-hydroxypyridine-5-carboxylic acid + NADH + O2 + H+
2-(acetamidomethylene)succinate + NAD+
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-
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
3-hydroxy-2-methylpyridine-5-carboxylate + NADPH + H+ + O2
2-(acetamidomethylene)succinate + NADP+
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?
5-hydroxynicotinic acid + NADH + O2 + H+
2-(formylamidomethylene)succinate + NAD+
about 100% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
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-
?
5-pyridoxic acid + NADH + O2 + H+
2-(acetamidomethylene)-beta-hydroxymethyl succinate + NAD+
5% of the activity with 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
additional information
?
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3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + H+ + O2
2-(acetamidomethylene)succinate + NAD+
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?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
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inducible enzyme opens the pyridine ring during the metabolic degradation of vitamin B6
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-
?
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
2-(acetamidomethylene)succinate + NAD+
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enzyme is involved in degradation of vitamin B6
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?
additional information
?
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also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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?
additional information
?
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also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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-
?
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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-
?
additional information
?
-
also catalyzes the NADH oxidation reaction uncoupled with ring opening in the absence of 2-methyl-3-hydroxypyridine-5-carboxylic acid
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-
?
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FAD
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FAD
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contains 2 mol of FAD per mol of enzyme
FAD
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contains 2 mol of FAD per mol of tetrameric enzyme. 412 nM
FAD
contains one FAD per subunit, tetrameric enzyme
FAD
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investigation of reaction using various FAD analogs
FAD
Km value 624 nM, one mol of the enzyme contains 1.93 mol of FAD
NADH
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NADH
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interacts with the holoenzyme in a slow catalytically irrelevant manner
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additional information
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no metal ion required
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5-hydroxynicotinic acid
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6-methylnicotinic acid
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competitive with 3-hydroxy-2-methylpyridine-5-carboxylate
NAD+
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binds competitively with O2, but not with NADH
p-chloromercuribenzoate
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0.05 mM, quick and complete inhibition
5-pyridoxic acid
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competitive with 3-hydroxy-2-methylpyridine-5-carboxylate
5-pyridoxic acid
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competitive
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0.0254
3-Hydroxy-2-methylpyridine-5-carboxylate
pH 8.0, 25°C
0.045 - 0.21
5-hydroxynicotinic acid
0.00056 - 0.0011
N-methyl-5-hydroxynicotinic acid
0.045
5-hydroxynicotinic acid
mutant enzyme Y270A, at pH 8.0 and 25°C
0.0589
5-hydroxynicotinic acid
pH 8.0, 25°C
0.06
5-hydroxynicotinic acid
wild type enzyme, at pH 8.0 and 25°C
0.065
5-hydroxynicotinic acid
recombinant enzyme
0.068
5-hydroxynicotinic acid
wild-type enzyme
0.21
5-hydroxynicotinic acid
mutant enzyme Y270F, at pH 8.0 and 25°C
0.00056
N-methyl-5-hydroxynicotinic acid
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calculation from stopped-flow data
0.0011
N-methyl-5-hydroxynicotinic acid
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calculation from steady-state data
0.0054
NADH
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calculation from steady-state data
0.1
NADH
wild type enzyme, at pH 8.0 and 25°C
0.12
NADH
mutant enzyme Y270F, at pH 8.0 and 25°C
0.18
NADH
recombinant enzyme
0.205
NADH
wild-type enzyme
0.47
NADH
mutant enzyme Y270A, at pH 8.0 and 25°C
0.0059
O2
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calculation from stopped-flow data
0.0117
O2
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calculation from steady-state data
0.126
O2
wild-type enzyme
0.148
O2
recombinant enzyme
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11.8
3-Hydroxy-2-methylpyridine-5-carboxylate
pH 8.0, 25°C
0.05 - 1300
5-hydroxynicotinic acid
additional information
additional information
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0.05
5-hydroxynicotinic acid
mutant enzyme Y270A, at pH 8.0 and 25°C
10.7
5-hydroxynicotinic acid
pH 8.0, 25°C
19
5-hydroxynicotinic acid
mutant enzyme Y270F, at pH 8.0 and 25°C
1300
5-hydroxynicotinic acid
wild type enzyme, at pH 8.0 and 25°C
additional information
additional information
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-
-
additional information
additional information
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-
-
additional information
additional information
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-
additional information
additional information
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1.1 - 22000
5-hydroxynicotinic acid
1.1
5-hydroxynicotinic acid
mutant enzyme Y270A, at pH 8.0 and 25°C
91
5-hydroxynicotinic acid
mutant enzyme Y270F, at pH 8.0 and 25°C
22000
5-hydroxynicotinic acid
wild type enzyme, at pH 8.0 and 25°C
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0.023
5-pyridoxic acid
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-
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0.48
5-hydroxynicotinic acid
Mesorhizobium loti
wild type enzyme, at pH 8.0 and 25°C
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7
substrate 3-hydroxy-2-methylpyridine-5-carboxylate
8
substrate 5-hydroxynicotinic acid
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20
79% of maximum activity
40
82% of maximum activity
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SwissProt
brenda
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brenda
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brenda
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SwissProt
brenda
MAFF303099, ATCC 700743
SwissProt
brenda
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brenda
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SwissProt
brenda
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brenda
MA-1
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brenda
MA-1
Uniprot
brenda
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physiological function
conversion of 2-methyl-3-hydroxypyridine-5-carboxylic acid to alpha-(N-acetylaminomethylene)succinic acid is the essential ring-opening step in the bacterial degradation of vitamin B6. The rearomatisation of the hydroxylated intermediate occurs spontaneously in aqueous solution. This implies that the ring-opening process occurs inside the enzyme's active site. Proposal of two pathways with reasonable energy barriers
physiological function
MHPCO is essential for the assimilation of pyridoxine, but not for its growth in a nutrient-rich medium. MHPCO is dispensable for at least nodule formation on roots of seedlings in symbiosis
physiological function
-
conversion of 2-methyl-3-hydroxypyridine-5-carboxylic acid to alpha-(N-acetylaminomethylene)succinic acid is the essential ring-opening step in the bacterial degradation of vitamin B6. The rearomatisation of the hydroxylated intermediate occurs spontaneously in aqueous solution. This implies that the ring-opening process occurs inside the enzyme's active site. Proposal of two pathways with reasonable energy barriers
physiological function
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MHPCO is essential for the assimilation of pyridoxine, but not for its growth in a nutrient-rich medium. MHPCO is dispensable for at least nodule formation on roots of seedlings in symbiosis
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O08453_9PROT
379
0
41772
TrEMBL
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Q988D3_RHILO
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
379
0
41748
TrEMBL
-
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Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
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160000
-
equilibrium sedimentation
166000
-
equilibrium sedimentation
41700
4 * 41700, calculation from nucleotide sequence
43000
-
4 * 43000, SDS-PAGE
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homodimer
crystal structure, the tetramer may have been disrupted
tetramer
4 * 42000, SDS-PAGE, 4 * 41747, calculated
tetramer
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4 * 42000, SDS-PAGE, 4 * 41747, calculated
tetramer
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4 * 43000, SDS-PAGE
tetramer
-
crystallization data
tetramer
4 * 41700, calculation from nucleotide sequence
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density functional theory/molecular mechanics calculations show that the active-site residues Arg211 and Tyr223 have a minor effect on the reaction, while the peptide bond of Pro295-Ala296, the side chain of Tyr82 and several crystal water molecules affect the reaction energy profile considerably. The ring-opening pathway, in which an epoxy transition state is formed, is more favored than the direct C2-C3 cleavage pathway. Both the reaction barriers for the hydroxylation and the ring-opening pathways are sensitive to the quantum mechanics/molecular mechanics partitioning
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hanging drop vapor diffusion method, using 8% (w/v) PEG 8000, 0.1 M Tris-HCl, pH 8.5
structure of enzyme with and without substrates 2-methyl-3-hydroxypyridine-5-carboxylic acid, 5-hydroxynicotinic acid and 5-pyridoxic acid, and of mutant Y270F. Residue Y270 is located in the active site
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Y223E
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the mutant shows reduced activity compared to the wild type enzyme
Y223F
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the mutant shows reduced activity compared to the wild type enzyme
Y223H
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the mutant shows reduced activity compared to the wild type enzyme
Y223T
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the mutant shows reduced activity compared to the wild type enzyme
Y82F
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the mutant shows reduced activity compared to the wild type enzyme
Y82H
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the mutant shows reduced activity compared to the wild type enzyme
Y82R
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the mutant shows reduced activity compared to the wild type enzyme
Y270A
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270A
less than 0.1% of the pyridine ring cleavage capacity of wild-type
Y270F
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270F
about 1.5% of the pyridine ring cleavage capacity of wild-type
Y270A
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the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270A
-
less than 0.1% of the pyridine ring cleavage capacity of wild-type
Y270F
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the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270F
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about 1.5% of the pyridine ring cleavage capacity of wild-type
Y270A
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the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270A
-
less than 0.1% of the pyridine ring cleavage capacity of wild-type
Y270F
-
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270F
-
about 1.5% of the pyridine ring cleavage capacity of wild-type
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the enzyme is very sensitive to oxidation, it loses activity rapidly in absence of mercaptoethanol even at 4°C, it is further stabilized in presence of high concentrations of glycerol or by serum albumin
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439056
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-20°C, 50% glycerol, 0.1% 2-mercaptoethanol, 1 month
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Q-Sepharose column chromatography and G-25 Sephadex gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
His-tag, expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
expression in Escherichia coli
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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
Kishore, G.M.; Snell, E.E.
Interaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase with FAD, substrates, and analogues. Spectral and fluorescence investigations
J. Biol. Chem.
256
4234-4240
1981
Pseudomonas sp.
brenda
Kishore, G.M.; Snell, E.E.
Kinetic investigations on a flavoprotein oxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
J. Biol. Chem.
256
4228-4233
1981
Pseudomonas sp.
brenda
Chaiyen, P.; Ballou, D.P.; Massey, V.
Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Proc. Natl. Acad. Sci. USA
94
7233-7238
1997
Pseudomonas sp. (O08453), Pseudomonas sp.
brenda
Chaiyen, P.; Brissette, P.; Ballou, D.P.; Massey, V.
Reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase with N-methyl-5-hydroxynicotinic acid: studies on the mode of binding, and Protonation Status of the Substrate
Biochemistry
36
13856-13864
1997
Pseudomonas sp.
brenda
Chaiyen, P.; Brissette, P.; Ballou, D.P.; Massey, V.
Unusual mechanism of oxygen atom transfer and product rearrangement in the catalytic reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Biochemistry
36
8060-8070
1997
Pseudomonas sp.
brenda
Chaiyen, P.; Brissette, P.; Ballou, D.P.; Massey, V.
Thermodynamics and reduction kinetics properties of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Biochemistry
36
2612-2621
1997
Pseudomonas sp.
brenda
Oonanant, W.; Sucharitakul, J.; Yuvaniyama, J.; Chaiyen, P.
Crystallization and preliminary x-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1
Acta Crystallogr. Sect. F
61
312-314
2005
Pseudomonas sp.
brenda
Chaiyen, P.; Sucharitakul, J.; Svasti, J.; Entsch, B.; Massey, V.; Ballou, D.P.
Use of 8-substituted-FAD analogues to investigate the hydroxylation mechanism of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
Biochemistry
43
3933-3943
2004
Pseudomonas sp.
brenda
McCulloch, K.; Mukherjee, T.; Begley, T.; Ealick, S.
Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications
Biochemistry
48
4139-4149
2009
Mesorhizobium loti (Q988D3)
brenda
Tian, B.; Strid, A.; Eriksson, L.A.
Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study
J. Phys. Chem. B
115
1918-1926
2011
Mesorhizobium loti, Mesorhizobium loti MAFF303099
brenda
Luanloet, T.; Sucharitakul, J.; Chaiyen, P.
Selectivity of substrate binding and ionization of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
FEBS J.
282
3107-3125
2015
Pseudomonas sp. MA-1
brenda
Kobayashi, J.; Yoshida, H.; Yagi, T.; Kamitori, S.; Hayashi, H.; Mizutani, K.; Takahashi, N.; Mikami, B.
Role of the Tyr270 residue in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti
J. Biosci. Bioeng.
123
154-162
2017
Mesorhizobium loti (Q988D3), Mesorhizobium loti, Mesorhizobium loti MAFF 303099 (Q988D3), Mesorhizobium loti MAFF303099 (Q988D3)
brenda
Tian, B.; Tu, Y.; Strid, A.; Eriksson, L.A.
Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase a theoretical study
Chemistry
16
2557-2566
2010
Mesorhizobium loti (Q988D3), Mesorhizobium loti MAFF 303099 (Q988D3)
brenda
Yuan, B.; Yokochi, N.; Yoshikane, Y.; Ohnishi, K.; Yagi, T.
Molecular cloning, identification and characterization of 2-methyl-3-hydroxypyridine-5-carboxylic-acid-dioxygenase-coding gene from the nitrogen-fixing symbiotic bacterium Mesorhizobium loti
J. Biosci. Bioeng.
102
504-510
2006
Mesorhizobium loti (Q988D3), Mesorhizobium loti, Mesorhizobium loti MAFF 303099 (Q988D3)
brenda
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