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Information on EC 1.2.1.100 - 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase and Organism(s) Mesorhizobium japonicum and UniProt Accession Q988C8

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IUBMB Comments
The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6).
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Mesorhizobium japonicum
UNIPROT: Q988C8
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The taxonomic range for the selected organisms is: Mesorhizobium japonicum
The enzyme appears in selected viruses and cellular organisms
Synonyms
5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate:NAD+ 5-oxidoreductase
The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
show the reaction diagram
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additional information
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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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NAD+ + H2O
3-hydroxy-2-methylpyridine-4,5-dicarboxylate + NADH + H+
show the reaction diagram
-
-
-
?
additional information
?
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme additionally catalyzes the reaction of 4-pyridoxic acid dehydrogenase
UniProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mugo, A.N.; Kobayashi, J.; Mikami, B.; Yoshikane, Y.; Yagi, T.; Ohnishi, K.
Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD+-dependent dismutase from Mesorhizobium loti
Biochem. Biophys. Res. Commun.
456
35-40
2015
Mesorhizobium japonicum (Q988C8)
Manually annotated by BRENDA team