Data extracted from this reference:
Engineering
E149Q
mutant shows a showed a different pH optimum depending on the cosubstrate. With NAD+, the mutant shows very low activity with an optimum pH at 8.5 in the universal buffer. In contrast, the optimum pH is 5.5 with NADH
Mesorhizobium loti
H137L
almost complete loss of activity
Mesorhizobium loti
KM Value [mM]
0.0058
NAD+
mutant E149Q, pH 8.0, 30°C
Mesorhizobium loti
0.0343
NAD+
wild-type, pH 8.0, 30°C
Mesorhizobium loti
0.0428
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
wild-type, pH 8.0, 30°C
Mesorhizobium loti
0.241
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
mutant E149Q, pH 8.0, 30°C
Mesorhizobium loti
Molecular Weight [Da]
59100
gel filtration
Mesorhizobium loti
Organism
Mesorhizobium loti
Q988H5
enzyme additionally catalyzes the reaction of 4-pyridoxic acid dehydrogenase
Mesorhizobium loti MAFF303099
Q988H5
enzyme additionally catalyzes the reaction of 4-pyridoxic acid dehydrogenase
Substrates and Products (Substrate)
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
745236
Mesorhizobium loti
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
?
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
745236
Mesorhizobium loti MAFF303099
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
?
additional information
enzyme catalyzes practically irreversible oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NAD+ to 3-hydroxy-2-methyl-pyridine 4, 5-dicarboxylic acid, and practically irreversible reduction of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NADH to 4-pyridoxic acid, i.e. reaction of EC 4-pyridoxic acid dehydrogenase. When the enzyme reaction is started with the combination of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NAD+ or that of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NADH, 3-hydroxy-2-methylpyridine-4,5-dicarboxylate and 4-pyridoxic acid are produced in an almost equimolar ratio throughout the reaction
745236
Mesorhizobium loti
?
additional information
enzyme catalyzes practically irreversible oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NAD+ to 3-hydroxy-2-methyl-pyridine 4, 5-dicarboxylic acid, and practically irreversible reduction of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NADH to 4-pyridoxic acid, i.e. reaction of EC 4-pyridoxic acid dehydrogenase. When the enzyme reaction is started with the combination of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NAD+ or that of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NADH, 3-hydroxy-2-methylpyridine-4,5-dicarboxylate and 4-pyridoxic acid are produced in an almost equimolar ratio throughout the reaction
745236
Mesorhizobium loti MAFF303099
?
Subunits
dimer
2 * 38900, SDS-PAGE, 2 * 33060, calculated from sequence, 2 * 33121, TOF-MS
Mesorhizobium loti
Synonyms
mlr6739
Mesorhizobium loti
Temperature Optimum [°C]
Turnover Number [1/s]
25
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
mutant E149Q, pH 8.0, 30°C
Mesorhizobium loti
204
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
wild-type, pH 8.0, 30°C
Mesorhizobium loti
pH Optimum
Engineering (protein specific)
E149Q
mutant shows a showed a different pH optimum depending on the cosubstrate. With NAD+, the mutant shows very low activity with an optimum pH at 8.5 in the universal buffer. In contrast, the optimum pH is 5.5 with NADH
Mesorhizobium loti
H137L
almost complete loss of activity
Mesorhizobium loti
KM Value [mM] (protein specific)
0.0058
NAD+
mutant E149Q, pH 8.0, 30°C
Mesorhizobium loti
0.0343
NAD+
wild-type, pH 8.0, 30°C
Mesorhizobium loti
0.0428
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
wild-type, pH 8.0, 30°C
Mesorhizobium loti
0.241
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
mutant E149Q, pH 8.0, 30°C
Mesorhizobium loti
Molecular Weight [Da] (protein specific)
59100
gel filtration
Mesorhizobium loti
Substrates and Products (Substrate) (protein specific)
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
745236
Mesorhizobium loti
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
?
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
745236
Mesorhizobium loti MAFF303099
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
?
additional information
enzyme catalyzes practically irreversible oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NAD+ to 3-hydroxy-2-methyl-pyridine 4, 5-dicarboxylic acid, and practically irreversible reduction of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NADH to 4-pyridoxic acid, i.e. reaction of EC 4-pyridoxic acid dehydrogenase. When the enzyme reaction is started with the combination of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NAD+ or that of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NADH, 3-hydroxy-2-methylpyridine-4,5-dicarboxylate and 4-pyridoxic acid are produced in an almost equimolar ratio throughout the reaction
745236
Mesorhizobium loti
?
additional information
enzyme catalyzes practically irreversible oxidation of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NAD+ to 3-hydroxy-2-methyl-pyridine 4, 5-dicarboxylic acid, and practically irreversible reduction of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate by NADH to 4-pyridoxic acid, i.e. reaction of EC 4-pyridoxic acid dehydrogenase. When the enzyme reaction is started with the combination of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NAD+ or that of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate and NADH, 3-hydroxy-2-methylpyridine-4,5-dicarboxylate and 4-pyridoxic acid are produced in an almost equimolar ratio throughout the reaction
745236
Mesorhizobium loti MAFF303099
?
Subunits (protein specific)
dimer
2 * 38900, SDS-PAGE, 2 * 33060, calculated from sequence, 2 * 33121, TOF-MS
Mesorhizobium loti
Temperature Optimum [°C] (protein specific)
Turnover Number [1/s] (protein specific)
25
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
mutant E149Q, pH 8.0, 30°C
Mesorhizobium loti
204
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
wild-type, pH 8.0, 30°C
Mesorhizobium loti
pH Optimum (protein specific)
General Information
physiological function
contrary to wild-type, mlr6793-disruptant cells cannot grow on pyridoxine, 4-pyridoxic acid or 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate as sole carbon and nitrogen source
Mesorhizobium loti
General Information (protein specific)
physiological function
contrary to wild-type, mlr6793-disruptant cells cannot grow on pyridoxine, 4-pyridoxic acid or 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate as sole carbon and nitrogen source
Mesorhizobium loti
Other publictions for EC 1.2.1.100
744227
Mugo
Crystal structure of 5-formyl ...
Mesorhizobium japonicum
Biochem. Biophys. Res. Commun.
456
35-40
2015
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745236
Yokochi
Gene identification and chara ...
Mesorhizobium loti, Mesorhizobium loti MAFF303099
J. Biochem.
145
493-503
2009
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745254
Lee
Enzymes of vitamin B6 degrada ...
Pseudomonas sp. MA-1
J. Biol. Chem.
261
15106-15111
1986
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