Information on EC 1.1.1.107 - pyridoxal 4-dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.107
-
RECOMMENDED NAME
GeneOntology No.
pyridoxal 4-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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vitamin B6 degradation
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Vitamin B6 metabolism
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SYSTEMATIC NAME
IUBMB Comments
pyridoxal:NAD+ 4-oxidoreductase
The enzyme acts on the hemiacetal form of the substrate.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-39-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
strain YK-1
Swissprot
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase enzyme family
physiological function
-
the enzyme is involved in the degradation pathway I of pyridoxine, a vitamin B6 compound
additional information
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structure analysis, homology modeling using the crystal structure of (S)-1-phenylethanol dehydrogenase, PDB ID 2EW8, molecular replacement, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-demethyl-2-ethylpyridoxal + NAD+
? + NADH
show the reaction diagram
D-arabinose + NAD+
? + NADH
show the reaction diagram
L-fucose + NAD+
? + NADH
show the reaction diagram
L-xylose + NAD+
? + NADH
show the reaction diagram
pyridine-4-aldehyde + NAD+
4-pyridoxolactone + NADH + H+
show the reaction diagram
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0.9% of the activity against pyridoxal
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-
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
show the reaction diagram
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
show the reaction diagram
additional information
?
-
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
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
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4-pyridoxate
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4-Pyridoxolactone
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8-hydroxyquinoline
m-phenanthroline
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o-phenanthroline
p-phenanthroline
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pyridoxal
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substrate inhibition, 90% inhibition at 2 mM
pyridoxamine
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pyridoxine
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Quinoline
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-Deoxypyridoxal
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stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.91
D-arabinose
pH 8.0, 30C
0.41
L-fucose
pH 8.0, 30C
3.5
L-Xylose
pH 8.0, 30C
0.042 - 0.29
NAD+
0.58 - 1.41
NADP+
0.076 - 13
pyridoxal
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
175
D-arabinose
Microbacterium luteolum
Q76KC2
pH 8.0, 30C
125
L-fucose
Microbacterium luteolum
Q76KC2
pH 8.0, 30C
214
L-Xylose
Microbacterium luteolum
Q76KC2
pH 8.0, 30C
136
NAD+
Mesorhizobium loti
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30C, pH 9.2; pH 9.2, 30C
59.2 - 149
pyridoxal
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13.7
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Escherichia coli BL21(DE3) cells transformed with pET21a-adh-pld
47.6
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Escherichia coli BL21(DE3) cells transformed with pET21a-pld
103.9
selenomethionine-substituted enzyme, 30C, pH 9.2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
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sodium phosphate buffer
8.5
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MOPS buffer
9.2
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; 50 mM CHES-NaOH buffer
9.3 - 9.5
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9.5
substrate L-fucose
additional information
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inactivation at low pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
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not active below
8.6 - 10
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pH 8.6: 66% of maximal activity, pH 10.0: 57% of maximal activity, 50 mM CHES-NaOH buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
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30C: 37% of maximal activity, 55C: 33% of maximal activity
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25531
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4 * 25531, calculated from sequence
80000
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gel filtration
84000
gel filtration
97000
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gel filtration
98000
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non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 26000, SDS-PAGE
tetramer
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4 * 25531, calculated from sequence; 4 * 26000; 4 * 26000, SDS-PAGE
additional information
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N-terminal amino acid analysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant selenomethionine-substituted enzyme, crystallized by the sitting-drop vapour-diffusion method using PEG 4000 as precipitant, in the presence of 0.45 mM NAD+. The crystals diffract to 2.9 A resolution and belong to the monoclinic space group P21
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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10 min, 1.3% of original activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 1% 2-mercaptoethanol, 24 h, no loss of activity, 2-mercaptoethanol is essential for stability
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant
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recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed from pET21a vector in Escherichia coli BL21(DE3)
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expression in Escherichia coli
expression in Escherichia coli; recombinant enzyme expressed in Escherichia coli
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overexpression in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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the enzyme is useful in determination of vitamin B6 contents, method development, overview
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