We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The taxonomic range for the selected organisms is: Citrobacter freundii The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
1,3-propanediol oxidoreductase, 1,3-propanediol dehydrogenase, 1,3-pd oxidoreductase,
lr_1734 ,
lr_0030 , 1,3-pd dehydrogenase, 1,3-propanediol-oxidoreductase, nadh-dependent 1,3-propanediol oxidoreductase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,3-propanediol oxidoreductase
-
1,3-PD:NAD+ oxidoreductase
-
-
-
-
1,3-propanediol dehydrogenase
-
-
-
-
1,3-propanediol oxidoreductase
-
-
-
-
1,3-propanediol-oxydoreductase
-
-
1,3-propanediol:NAD oxidoreductase
-
-
-
-
3-hydroxypropionaldehyde reductase
-
-
-
-
dehydrogenase, 1,3-propanediol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
propane-1,3-diol:NAD+ 1-oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1-butanol + NAD+
NADH + butanal
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
NADH + propanal
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
2,3-butanediol + NAD+
? + NADH
-
-
-
-
r
2-butanol + NAD+
NADH + butanone
-
-
-
-
?
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
r
ethanol + NAD+
NADH + ethanal
-
-
-
-
r
ethylene glycol + NAD+
NADH + ?
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
propane-1,2-diol + NAD+
2-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
PDOR requires NAD(H) as a cofactor, but the highly conserved NAD(H) binding fingerprint pattern G-X-G-X-X-G is not present in the amino acid sequence
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
-
-
Fe2+
-
required, activates
Mn2+
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8.9 - 10.05
3-hydroxypropanal
1.28
Propane-1,3-diol
pH 10.5, 25°C
1.25
Propane-1,3-diol
-
-
additional information
additional information
Michaelis-Menten kinetics
-
8.9
3-hydroxypropanal
pH and temperature not specified in the publication
10.05
3-hydroxypropanal
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
49.5
reduction of 3-hydroxypropanal, pH 8.0, 37°C
77.9
oxidation of propane-1,3-diol, pH 10.5, 25°C
11
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10.5
oxidation of alcohol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7
less than 10% of maximum activity for oxidation reaction
7 - 8.5
more than 80% of maximum activity for reduction of aldehyde
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
enzyme PDOR shows high similarity with member of the family of type III alcohol dehydrogenases. PDOR requires NAD(H) as a cofactor, but the highly conserved NAD(H) binding fingerprint pattern G-X-G-X-X-G is not present in the amino acid sequence. This is also characteristic of most type III alcohol dehydrogenases
metabolism
1,3-propanediol oxidoreductase (PDOR) is the rate-limiting enzyme in 1,3-propandiol synthesis biological pathway. 3-Hydroxypropanal is an intermediary metabolite in the 1,3-propanediol synthesis pathway. It is also an inhibitor to the activity of glycerol dehydratase (GDHt) and PDOR. PDOR is the key rate-limiting enzyme of the 3-HPA transformation and 1,3-PD formation when high concentration of glycerol is used in fermentation
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
malfunction
-
accumulation of 3-hydroxypropanal can inhibit the activity of glycerol dehydratase to prevent the growth of bacteria and result in reducing the production of propane-1,3-diol, leading to a major influence in the production of propane-1,3-diol
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DHAT_CITFR
387
0
41482
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
42000
x * 42000, SDS-PAGE
440000
recombinant His6-tagged enzyme, gel filtration
331000
-
gel filtration, sedimentation coefficient
43400
-
-
43400
-
8 * 43400, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homodecamer
10 * 42927, sequence calculation, 10 * 43000, recombinant His6-tagged enzyme, SDS-PAGE
octamer
-
8 * 43400, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli
gene dhaT, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene dhaT, part of the dha regulon, genetic structure, recombinant expression in Escherichia coli
-
overexpression in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
synthesis
-
the enzyme can be used for 1,3-propandiol synthesis for use in resaerch and industrial applications, especially in biodiesel industry, but also as a monomer for polycondensation to manufacture plastics with special properties, i.e., polyesters, polyethers, polyurethanes, and polytrimethylene terephthalate as a monomer for cyclic compounds, and as a polyglycol-type lubricant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Daniel, R.; Boenigk, R.; Gottschalk, G.
Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii and cloning, sequencing, and overexpression of the corresponding gene in Escherichia coli
J. Bacteriol.
177
2151-2156
1995
Citrobacter freundii
brenda
Qi, X.; Deng, W.; Wang, F.; Guo, Q.; Chen, H.; Wang, L.; He, X.; Huang, R.
Molecular cloning, co-expression, and characterization of glycerol dehydratase and 1,3-propanediol dehydrogenase from Citrobacter freundii
Mol. Biotechnol.
54
469-474
2013
Citrobacter freundii (P45513), Citrobacter freundii
brenda
Jiang, W.; Wang, S.; Wang, Y.; Fang, B.
Key enzymes catalyzing glycerol to 1,3-propanediol
Biotechnol. Biofuels
9
57
2016
Citrobacter freundii, Citrobacter freundii DSM 30040, Clostridium butyricum, Clostridium butyricum E5, Clostridium pasteurianum, Clostridium perfringens, Klebsiella pneumoniae, Klebsiella pneumoniae DSM2026, Lentilactobacillus buchneri, Levilactobacillus brevis, Limosilactobacillus reuteri, Pantoea agglomerans, Thermotoga maritima
brenda
Qi, X.; Zhu, J.; Luo, Y.; Lin, J.; Wang, X.; Ju, Z.; Chen, F.; Zhu, X.; Chen, H.; Sun, W.; Wang, L.
Overexpression and characterization of the gene encoding 1,3-propanediol oxidoreductase of Citrobacter freundii
Key Eng. Mater.
636
121-124
2014
Citrobacter freundii (P45513)
-
brenda