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Information on EC 1.1.1.202 - 1,3-propanediol dehydrogenase and Organism(s) Citrobacter freundii and UniProt Accession P45513

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Citrobacter freundii
UNIPROT: P45513 not found.
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
propane-1,3-diol:NAD+ 1-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
81611-70-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
show the reaction diagram
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
show the reaction diagram
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH
show the reaction diagram
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
show the reaction diagram
-
-
-
-
r
1-butanol + NAD+
NADH + butanal
show the reaction diagram
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
show the reaction diagram
-
-
-
-
r
1-propanol + NAD+
NADH + propanal
show the reaction diagram
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
show the reaction diagram
-
-
-
-
r
2,3-butanediol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
r
2-butanol + NAD+
NADH + butanone
show the reaction diagram
-
-
-
-
?
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
show the reaction diagram
-
-
-
-
r
ethanol + NAD+
NADH + ethanal
show the reaction diagram
-
-
-
-
r
ethylene glycol + NAD+
NADH + ?
show the reaction diagram
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
propane-1,2-diol + NAD+
2-hydroxypropanal + NADH
show the reaction diagram
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
show the reaction diagram
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
show the reaction diagram
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
show the reaction diagram
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
show the reaction diagram
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
show the reaction diagram
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
show the reaction diagram
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
show the reaction diagram
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.9 - 10.05
3-hydroxypropanal
1.28
Propane-1,3-diol
pH 10.5, 25°C
0.033
NADH
-
-
1.25
Propane-1,3-diol
-
-
11
propionaldehyde
-
-
additional information
additional information
Michaelis-Menten kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5
oxidation of alcohol
8
reduction of aldehyde
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
less than 10% of maximum activity for oxidation reaction
7 - 8.5
more than 80% of maximum activity for reduction of aldehyde
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
oxidation of alcohol
37
reduction of aldehyde
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHAT_CITFR
387
0
41482
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
x * 42000, SDS-PAGE
440000
recombinant His6-tagged enzyme, gel filtration
331000
-
gel filtration, sedimentation coefficient
43400
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, SDS-PAGE
homodecamer
10 * 42927, sequence calculation, 10 * 43000, recombinant His6-tagged enzyme, SDS-PAGE
octamer
-
8 * 43400, SDS-PAGE
oligomer
-
x * 43400
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team