Any feedback?
No. of entries
Information on EC 1.1.1.107 - pyridoxal 4-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.107
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.107 pyridoxal 4-dehydrogenase
IUBMB Comments
The enzyme acts on the hemiacetal form of the substrate.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 1.1.1.107
- pyridoxine
- luteolum
-
mesorhizobium
- 5'-phosphate
- loti
- chaperonin
-
monoclinic
-
4-oxidase
- nadp+
-
sitting-drop
-
4-pyridoxic
- microbacterium
-
vapour-diffusion
- analysis
showSynonyms
pyridoxal 4-dehydrogenase, pyridoxal dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PLDH
pyridoxal dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
vitamin B6 degradation I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
pyridoxal:NAD+ 4-oxidoreductase
The enzyme acts on the hemiacetal form of the substrate.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37250-39-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-fucose + NAD+
L-fucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
pyridine-4-aldehyde + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: 0.9% of the activity against pyridoxal
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: cells coexpressing pyridoxal 4-dehydrogenase and alcohol dehydrogenase show a higher conversion rate than those expressing pyridoxal 4-dehydrogenase alone
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: cells coexpressing pyridoxal 4-dehydrogenase and alcohol dehydrogenase show a higher conversion rate than those expressing pyridoxal 4-dehydrogenase alone
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: 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
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: via pyridoxal hemiacetal
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: 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
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
Substrates: -
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: specific conversion of vitamin B6
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: development and evaluation of a method to determine vitamin B6, pyridoxal, involving the enzyme, overview
Products: -
Products: -
ir
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
pyridoxal + NADP+
4-pyridoxolactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: pyridoxal-5-phosphate, pyridoxamine, pyridoxine, 2-nitrobenzaldehyde, 3-nitrobenzaldehyde, 4-nitrobenzaldehyde, o-phthalaldehyde, 5-nitrosalicylaldehyde, 2-carboxybenzaldehyde
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for assimilation of vitamin B6 compounds and is the second step enzyme in the degradation pathway for pyridoxine
Products: -
Products: -
?
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: PLDH is essential for the assimilation of vitamin B6 compounds and the second step enzyme in their degradation pathway
Products: -
Products: -
ir
pyridoxal + NAD+
4-pyridoxolactone + NADH + H+
-
Substrates: specific conversion of vitamin B6
Products: -
Products: -
ir
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.6 - 10
-
pH 8.6: 66% of maximal activity, pH 10.0: 57% of maximal activity, 50 mM CHES-NaOH buffer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
-
structure analysis, homology modeling using the crystal structure of (S)-1-phenylethanol dehydrogenase, PDB ID 2EW8, molecular replacement, overview
Show AA Sequence and Transmembrane Helices (736 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
38000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1% 2-mercaptoethanol, 24 h, no loss of activity, 2-mercaptoethanol is essential for stability
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is useful in determination of vitamin B6 contents, method development, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q76KC2), Microbacterium luteolum YK-1
brenda
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
brenda
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
brenda
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
brenda
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 (Q988B7), Mesorhizobium loti, 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
EXTERNAL LINKS (specific for EC-Number 1.1.1.107)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
