Information on EC 1.1.99.42 - 4-pyridoxic acid dehydrogenase

for references in articles please use BRENDA:EC1.1.99.42
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.99.42
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RECOMMENDED NAME
GeneOntology No.
4-pyridoxic acid dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-pyridoxate + acceptor = 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced acceptor
show the reaction diagram
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-
-
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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
4-pyridoxate:acceptor 5-oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme additionally catalyzes the reaction of EC 1.2.1.100
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
4-pyridoxate + 2,6-dichloroindophenol
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced 2,6-dichloroindophenol
show the reaction diagram
4-pyridoxate + NAD+
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NADH + H+
show the reaction diagram
4-pyridoxate + phenazine methosulfate
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced phenazine methosulfate
show the reaction diagram
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-
-
-
?
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NADH + H+
4-pyridoxate + NAD+
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
4-pyridoxate + 2,6-dichloroindophenol
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + reduced 2,6-dichloroindophenol
show the reaction diagram
4-pyridoxate + NAD+
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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not inhibitory: cyanide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0058 - 0.029
4-pyridoxate
0.02 - 0.03
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
0.0066
NAD+
pH 8.0, temperature not specified in the publication
0.0124 - 0.033
NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
4-pyridoxate
-
pH 8.0, temperature not specified in the publication
78 - 300
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate
0.01
NAD+
pH 8.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.9
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pH 8.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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54% of maximum activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
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sucrose density centrifugation
57000
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gel filtration
59100
gel filtration
61000
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and 63000, PAGE
63000
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and 61000, PAGE
additional information
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undenatured preparations aggregate readily, leading to mass values of 148,000, 470,000, and more than 670000 obtained by density gradient centrifugation or by gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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stable for 10 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, half-life 3 days in absence of glycerol. In presence of glycerol 0-20% of the activity is lost in 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from Pseudomonas MA-1 grown with pyridoxine as a sole source of carbon and nitrogen
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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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additional information