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Information on EC 1.1.1.107 - pyridoxal 4-dehydrogenase for references in articles please use BRENDA:EC1.1.1.107
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EC Tree
IUBMB Comments The enzyme acts on the hemiacetal form of the substrate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
pyridoxal dehydrogenase,
more
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pyridoxal dehydrogenase
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PLDH
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pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+
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pyridoxal:NAD+ 4-oxidoreductase
The enzyme acts on the hemiacetal form of the substrate.
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2-demethyl-2-ethylpyridoxal + NAD+
? + NADH
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?
D-arabinose + NAD+
? + NADH
pyridine-4-aldehyde + NAD+
4-pyridoxolactone + NADH + H+
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0.9% of the activity against pyridoxal
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
additional information
?
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D-arabinose + NAD+
? + NADH
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?
D-arabinose + NAD+
? + NADH
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?
L-fucose + NAD+
? + NADH
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?
L-fucose + NAD+
? + NADH
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?
L-xylose + NAD+
? + NADH
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?
L-xylose + NAD+
? + NADH
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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cells coexpressing pyridoxal 4-dehydrogenase and alcohol dehydrogenase show a higher conversion rate than those expressing pyridoxal 4-dehydrogenase alone
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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cells coexpressing pyridoxal 4-dehydrogenase and alcohol dehydrogenase show a higher conversion rate than those expressing pyridoxal 4-dehydrogenase alone
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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very low activity toward NADP+. 0.16% of the maximal activity obtained with NAD+ is observed when 5.0 mM NADP+ is used. The enzyme does not catalyze the reduction of 4-pyridoxolactone with NADH + H+ to pyridoxal even when a 100fold higher concentration of the enzyme is used for the reverse reaction
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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via pyridoxal hemiacetal
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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very low activity toward NADP+. 0.16% of the maximal activity obtained with NAD+ is observed when 5.0 mM NADP+ is used. The enzyme does not catalyze the reduction of 4-pyridoxolactone with NADH + H+ to pyridoxal even when a 100fold higher concentration of the enzyme is used for the reverse reaction
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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specific conversion of vitamin B6
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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development and evaluation of a method to determine vitamin B6, pyridoxal, involving the enzyme, overview
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ir
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
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pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
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?
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
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?
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
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?
additional information
?
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the enzyme shows less than 0.01% of the activity of pyridoxal toward pyridoxal 5'-phosphate (0.5 mM), pyridoxine (0.8 mM), and pyridoxamine, pyridoxamine 5'-phosphate, 4-phthalaldehyde, 2-nitrobenzaldehyde, 3-nitrobenzaldehyde, 4-nitrobenzaldehyde, pyridine, formaldehyde, and 2-carboxybenzaldehyde (1.0 mM each). The enzyme shows less than 0.01% of the activity of pyridoxal toward DL-glyceraldehyde, D-xylose, L-xylose, D-ribose, D-glucose, D-arabinose, L-arabinose, L-fucose, and D-galactose (250 mM each)
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additional information
?
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the enzyme shows less than 0.01% of the activity of pyridoxal toward pyridoxal 5'-phosphate (0.5 mM), pyridoxine (0.8 mM), and pyridoxamine, pyridoxamine 5'-phosphate, 4-phthalaldehyde, 2-nitrobenzaldehyde, 3-nitrobenzaldehyde, 4-nitrobenzaldehyde, pyridine, formaldehyde, and 2-carboxybenzaldehyde (1.0 mM each). The enzyme shows less than 0.01% of the activity of pyridoxal toward DL-glyceraldehyde, D-xylose, L-xylose, D-ribose, D-glucose, D-arabinose, L-arabinose, L-fucose, and D-galactose (250 mM each)
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additional information
?
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no substrate: pyridoxal-5’-phosphate, pyridoxamine, pyridoxine, 2-nitrobenzaldehyde, 3-nitrobenzaldehyde, 4-nitrobenzaldehyde, o-phthalaldehyde, 5-nitrosalicylaldehyde, 2-carboxybenzaldehyde
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pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
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?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
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specific conversion of vitamin B6
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ir
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NAD+
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pyridoxal
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substrate inhibition, 90% inhibition at 2 mM
8-hydroxyquinoline
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1 mM, 78% inhibition
o-phenanthroline
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1 mM, 15% inhibition
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5-Deoxypyridoxal
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stimulation
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0.91
D-arabinose
pH 8.0, 30°C
0.41
L-fucose
pH 8.0, 30°C
3.5
L-Xylose
pH 8.0, 30°C
0.042
NAD+
cosubstrate L-fucose, pH 8.0, 30°C
0.05
NAD+
cosubstrate pyridoxal, pH 8.0, 30°C
0.133
NAD+
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30°C, pH 8.0
0.28
NAD+
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30°C, pH 9.2; pH 9.2, 30°C
0.58
NADP+
cosubstrate L-fucose, pH 8.0, 30°C
1.41
NADP+
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30°C, pH 8.0
0.076
pyridoxal
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0.091
pyridoxal
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30°C, pH 9.2; pH 9.2, 30°C
0.473
pyridoxal
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30°C, pH 8.0
13
pyridoxal
pH 8.0, 30°C
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175
D-arabinose
pH 8.0, 30°C
125
L-fucose
pH 8.0, 30°C
214
L-Xylose
pH 8.0, 30°C
136
NAD+
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30°C, pH 9.2; pH 9.2, 30°C
59.2
pyridoxal
pH 8.0, 30°C
149
pyridoxal
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30°C, pH 9.2; pH 9.2, 30°C
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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, 30°C, pH 9.2
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8 - 8.5
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sodium phosphate buffer
9.2
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; 50 mM CHES-NaOH buffer
additional information
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inactivation at low pH
8
substrate pyridoxal
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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
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30
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30 - 55
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30°C: 37% of maximal activity, 55°C: 33% of maximal activity
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brenda
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Swissprot
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UniProt
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; MAFF303099
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UniProt
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MAFF303099
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Swissprot
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growth on pyridoxine as carbon and nitrogen source
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brenda
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evolution
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the enzyme belongs to the short-chain dehydrogenase/reductase enzyme family
physiological function
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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
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Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
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25531
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4 * 25531, calculated from sequence
98000
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non-denaturing PAGE
26000
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4 * 26000; 4 * 26000, SDS-PAGE
26000
x * 26000, SDS-PAGE
38000
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2 * 38000, SDS-PAGE
38000
2 * 38000, SDS-PAGE
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additional information
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N-terminal amino acid analysis
?
x * 26000, SDS-PAGE
?
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x * 26000, SDS-PAGE
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dimer
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2 * 38000, SDS-PAGE
dimer
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2 * 38000, SDS-PAGE
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tetramer
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4 * 25531, calculated from sequence; 4 * 26000; 4 * 26000, SDS-PAGE
tetramer
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4 * 25531, calculated from sequence; 4 * 26000; 4 * 26000, SDS-PAGE
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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
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60
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10 min, 1.3% of original activity
45
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10 min, stable below
45
10 min, 75% inactivation
50
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10 min, 76% of original activity
50
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10 min, no residual activity
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4°C, 1% 2-mercaptoethanol, 24 h, no loss of activity, 2-mercaptoethanol is essential for stability
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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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analysis
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the enzyme is useful in determination of vitamin B6 contents, method development, overview
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Burg, R.W.; Snell, E.E.
The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase
J. Biol. Chem.
244
2585-2589
1969
Pseudomonas sp.
brenda
Yokochi, N.; Yoshikane, Y.; Yagi, T.; Yamasaki, M.; Mikami, B.
Crystallization and preliminary X-ray analysis of pyridoxal 4-dehydrogenase, the second enzyme in degradation pathway I of pyridoxine
Acta Crystallogr. Sect. D
60
2061-2062
2004
Microbacterium luteolum
brenda
Trongpanich, Y.; Abe, K.; Kaneda, Y.; Morita, T.; Yagi, T.
Purification and characterization of pyridoxal 4-dehydrogenase from Aureobacterium luteolum
Biosci. Biotechnol. Biochem.
66
543-548
2002
Microbacterium luteolum
brenda
Yokochi, N.; Yoshikane, Y.; Trongpanich, Y.; Ohnishi, K.; Yagi, T.
Molecular cloning, expression, and properties of an unusual aldo-keto reductase family enzyme, pyridoxal 4-dehydrogenase, that catalyzes irreversible oxidation of pyridoxal
J. Biol. Chem.
279
37377-37384
2004
Microbacterium luteolum (Q76KC2), Microbacterium luteolum YK-1, Microbacterium luteolum YK-1 (Q76KC2)
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Yokochi, N.; Nishimura, S.; Yoshikane, Y.; Ohnishi, K.; Yagi, T.
Identification of a new tetrameric pyridoxal 4-dehydrogenase as the second enzyme in the degradation pathway for pyridoxine in a nitrogen-fixing symbiotic bacterium, Mesorhizobium loti
Arch. Biochem. Biophys.
452
1-8
2006
Mesorhizobium loti, Mesorhizobium loti MAFF303099
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Nishimura, S.; Nagano, S.; A Crai, C.; Yokochi, N.; Yoshikane, Y.; Ge, F.; Yagi, T.
Determination of individual vitamin B(6) compounds based on enzymatic conversion to 4-pyridoxolactone
J. Nutr. Sci. Vitaminol.
54
18-24
2008
Saccharomyces cerevisiae
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Tamura, A.; Yoshikane, Y.; Yokochi, N.; Yagi, T.
Synthesis of 4-pyridoxolactone from pyridoxine using a combination of transformed Escherichia coli cells
J. Biosci. Bioeng.
106
460-465
2008
Escherichia coli, Escherichia coli JM109
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Chu, H.N.; Kobayashi, J.; Yoshikane, Y.; Mikami, B.; Yagi, T.
Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti
Acta Crystallogr. Sect. F
66
718-720
2010
Mesorhizobium loti, Mesorhizobium loti (Q988B7), Mesorhizobium loti MAFF303099 (Q988B7)
brenda
Chu, H.N.; Kobayashi, J.; Mikami, B.; Yagi, T.
The crystal structure of SDR-type pyridoxal 4-dehydrogenase of Mesorhizobium loti
Biosci. Biotechnol. Biochem.
75
388-390
2011
Mesorhizobium loti
brenda
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