BRENDA - Enzyme Database
show all sequences of 1.2.1.100

Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD+-dependent dismutase from Mesorhizobium loti

Mugo, A.N.; Kobayashi, J.; Mikami, B.; Yoshikane, Y.; Yagi, T.; Ohnishi, K.; Biochem. Biophys. Res. Commun. 456, 35-40 (2015)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Mesorhizobium japonicum
Crystallization (Commentary)
Crystallization (Commentary)
Organism
structure determined by molecular replacement, to 1. 55 A resolution. Residues Ser116, His137 and Glu149 are connected by a hydrogen bonding network forming a catalytic triad
Mesorhizobium japonicum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
Mesorhizobium japonicum
-
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
-
-
?
additional information
Mesorhizobium japonicum
enzyme catalyzes oxidation of the hemiacetal form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 3-hydroxy-2-methylpyridine-4,5-dicarboxylate with NAD+ and reduction of an aldehyde form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 4-pyridoxic acid with NADH, i.e. reaction of 4-pyridoxic acid dehydrogenase. The Ser-His-Glu catalytic triad facilitates the two-way reactions. Ser116 assists protonation of His137 to drive the reduction reaction. His137 acts as a catalytic base to abstract a proton during oxidation. Glu149 likely neutralizes the positive charge on His137 after the deprotonation of the substrate
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Mesorhizobium japonicum
Q988C8
enzyme additionally catalyzes the reaction of 4-pyridoxic acid dehydrogenase
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
-
744227
Mesorhizobium japonicum
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
-
-
-
?
additional information
enzyme catalyzes oxidation of the hemiacetal form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 3-hydroxy-2-methylpyridine-4,5-dicarboxylate with NAD+ and reduction of an aldehyde form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 4-pyridoxic acid with NADH, i.e. reaction of 4-pyridoxic acid dehydrogenase. The Ser-His-Glu catalytic triad facilitates the two-way reactions. Ser116 assists protonation of His137 to drive the reduction reaction. His137 acts as a catalytic base to abstract a proton during oxidation. Glu149 likely neutralizes the positive charge on His137 after the deprotonation of the substrate
744227
Mesorhizobium japonicum
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
mlr6793
-
Mesorhizobium japonicum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Mesorhizobium japonicum
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Mesorhizobium japonicum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
structure determined by molecular replacement, to 1. 55 A resolution. Residues Ser116, His137 and Glu149 are connected by a hydrogen bonding network forming a catalytic triad
Mesorhizobium japonicum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
Mesorhizobium japonicum
-
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
-
-
?
additional information
Mesorhizobium japonicum
enzyme catalyzes oxidation of the hemiacetal form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 3-hydroxy-2-methylpyridine-4,5-dicarboxylate with NAD+ and reduction of an aldehyde form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 4-pyridoxic acid with NADH, i.e. reaction of 4-pyridoxic acid dehydrogenase. The Ser-His-Glu catalytic triad facilitates the two-way reactions. Ser116 assists protonation of His137 to drive the reduction reaction. His137 acts as a catalytic base to abstract a proton during oxidation. Glu149 likely neutralizes the positive charge on His137 after the deprotonation of the substrate
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
-
744227
Mesorhizobium japonicum
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
-
-
-
?
additional information
enzyme catalyzes oxidation of the hemiacetal form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 3-hydroxy-2-methylpyridine-4,5-dicarboxylate with NAD+ and reduction of an aldehyde form of 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate to 4-pyridoxic acid with NADH, i.e. reaction of 4-pyridoxic acid dehydrogenase. The Ser-His-Glu catalytic triad facilitates the two-way reactions. Ser116 assists protonation of His137 to drive the reduction reaction. His137 acts as a catalytic base to abstract a proton during oxidation. Glu149 likely neutralizes the positive charge on His137 after the deprotonation of the substrate
744227
Mesorhizobium japonicum
?
-
-
-
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Mesorhizobium japonicum
Other publictions for EC
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744227
Mugo
Crystal structure of 5-formyl ...
Mesorhizobium japonicum
Biochem. Biophys. Res. Commun.
456
35-40
2015
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1
1
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2
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3
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2
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1
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1
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-
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1
-
1
-
-
-
-
-
-
-
-
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2
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-
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2
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1
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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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-
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-
2
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4
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1
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5
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-
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4
1
1
1
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2
1
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2
-
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4
-
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1
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-
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-
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4
1
1
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2
1
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-
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1
1
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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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2
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1
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1
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2
1
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1
1
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2
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1
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2
1
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1
1
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1
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1
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