Information on EC 1.2.1.100 - 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase

for references in articles please use BRENDA:EC1.2.1.100
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.100
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RECOMMENDED NAME
GeneOntology No.
5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vitamin B6 degradation
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Vitamin B6 metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate:NAD+ 5-oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme additionally catalyzes the reaction of 4-pyridoxic acid dehydrogenase
UniProt
Manually annotated by BRENDA team
enzyme additionally catalyzes the reaction of 4-pyridoxic acid dehydrogenase
UniProt
Manually annotated by BRENDA team
enzyme additionally catalyzes the reaction of 4-pyridoxic acid dehydrogenase
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q988C8
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additional information
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Q988C8
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0428 - 0.241
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
0.0058 - 0.0343
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25 - 670
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59100
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced in response to growth on pyridoxine
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
H137L
almost complete loss of activity
E149Q
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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
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H137L
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almost complete loss of activity
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