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Information on EC 1.1.1.202 - 1,3-propanediol dehydrogenase
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1.1.1.202 1,3-propanediol dehydrogenaseSpecify your search results
Word Map
- 1.1.1.202
- pneumoniae
- klebsiella
- dehydratase
- synthesis
-
fed-batch
- butyricum
- citrobacter
- freundii
-
3-hydroxypropionic
-
dissimilation
-
eutropha
- pasteurianum
- reuteri
-
biodiesel
- 1,2-propanediol
- industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
(NADH)-linked 1,3-PD oxidoreductase, 1,3-PD dehydrogenase, 1,3-PD oxidoreductase, 1,3-PD-DH, 1,3-PD:NAD+ oxidoreductase, 1,3-PDDH, 1,3-Pdiol dehydrogenase, 1,3-propanediol dehydrogenase, 1,3-propanediol oxidoreductase, 1,3-propanediol-oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,3-PD dehydrogenase
1,3-PD oxidoreductase
1,3-PD:NAD+ oxidoreductase
-
-
-
-
1,3-PDDH
1,3-Pdiol dehydrogenase
1,3-propanediol dehydrogenase
-
-
-
-
1,3-propanediol oxidoreductase
1,3-propanediol-oxidoreductase
1,3-propanediol-oxydoreductase
1,3-propanediol:NAD oxidoreductase
-
-
-
-
3-hydroxypropionaldehyde reductase
-
-
-
-
ADH3
dehydrogenase, 1,3-propanediol
-
-
-
-
DhaT
NADH-dependent 1,3-PD dehydrogenase
NADH-dependent 1,3-propanediol oxidoreductase
PDOR
YqhD
1,3-propanediol oxidoreductase
-
-
-
-
1,3-propanediol oxidoreductase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
propane-1,3-diol + NAD+ = 3-hydroxypropanal + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
propane-1,3-diol:NAD+ 1-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
81611-70-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetone + NADH + H+
?
-
25.3% activity compared to propionaldehyde
-
-
?
hydroxyacetone + NADH + H+
?
-
30.6% activity compared to propionaldehyde
-
-
?
propane-1,3-diol + NADP+
3-hydroxypropanal + NADPH + H+
NADP+ is not substrate for wild-type, but for mutant D41G
-
-
r
1,3-propanediol + NAD+
3-hydroxypropanal + NADH
activity with 1,3-propanediol is highly dependent on the presence of Ni2+
-
-
?
1,3-propanediol + NAD+
3-hydroxypropanal + NADH
activity with 1,3-propanediol is highly dependent on the presence of Ni2+
-
-
?
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
r
3-hydroxypropanal + NADH
propane-1,3-diol + NAD+
-
overexpression of PDOR does not affect the concentration of propane-1,3-diol, but it enhances the molar yield from 50.6 to 64.0% and reduces the concentration of by-products, among them, the concentrations of lactic acid, ethanol and succinic acid are decreased by 51.8, 50.6 and 47.4%, respectively. Activity of recombinant PDOR is 44fold higher than those of the wild-type. PDOR overexpression leads to a slower cell growth and lower productivity, and during the fed-batch fermentation in 3.7 l bioreactor, a growth stagnation is observed
-
-
?
3-hydroxypropanal + NADH
propane-1,3-diol + NAD+
-
overexpression of PDOR does not affect the concentration of propane-1,3-diol, but it enhances the molar yield from 50.6 to 64.0% and reduces the concentration of by-products, among them, the concentrations of lactic acid, ethanol and succinic acid are decreased by 51.8, 50.6 and 47.4%, respectively. Activity of recombinant PDOR is 44fold higher than those of the wild-type. PDOR overexpression leads to a slower cell growth and lower productivity, and during the fed-batch fermentation in 3.7 l bioreactor, a growth stagnation is observed
-
-
?
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
part of the conversion of glycerol to 1,3-propanediol, not the limiting step
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
3-hydroxypropionaldehyde is an inhibitory intermediary metabolite in the 1,3-propanediol synthesis pathway during fermentation of raw material required for the synthesis of polytrimethylene terephthalate and other polyester fibers, accumulation of 3-hydroxypropanal in broth causes an irreversible cessation of the fermentation process
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
a key enzyme in the reductive pathway of anaerobic glycerol dissimilation converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
activity of PDOR in KG1 (pUC18K-dhaT) is 44fold higher than that of the wild-type strain. In the resting cell system, overexpression of 1,3-propanediol oxidoreductase leads to faster glycerol conversion and propane-1,3-diol production. After a 12 h conversion process, it improves the yield of propane-1,3-diol by 20.4% and enhances the conversion ratio of glycerol into propane-1,3-diol from 50.8% to 59.8%
-
-
?
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
in the cell exponential growth phase, the reaction catalyzed by 1,3-propanediol oxidoreductase is the rate limiting step in 1,3-propanediol production
-
-
?
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
level of PDOR activity of Klebsiella pneumoniae/pETPkan-dhaT (1.64 U/mg) shows an increase of 0.9fold in PDOR activity with respect to the wild-type Klebsiella pneumoniae (0.85 U/mg). The recombinant strain Klebsiella pneumoniae/pETPkan-dhaT improves propane-1,3-diol production by 16.5% with respect to the wild-type strain
-
-
?
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
overexpression of PDOR increases activity by 3.2fold, enzyme activity ratio of PDOR/GDHt (glycerol dehydratase) also is increased. 3-hydroxypropanal accumulation is successfully decreased and the risk of fermentation cease is reduced at the same time by overexpression of PDOR and GDH (glycerol dehydrogenase)
-
-
?
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
under physiological conditions, DhaT mostly catalyzes the forward reaction
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
under physiological conditions, DhaT mostly catalyzes the forward reaction
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
3-hydroxypropionaldehyde is an inhibitory intermediary metabolite in the 1,3-propanediol synthesis pathway during fermentation of raw material required for the synthesis of polytrimethylene terephthalate and other polyester fibers, accumulation of 3-hydroxypropanal in broth causes an irreversible cessation of the fermentation process
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction, 3-hydroxypropanal is the preferred substrate
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction, 3-hydroxypropanal is the preferred substrate
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-
r
3-hydroxypropanal + NADPH + H+
propane-1,3-diol + NADP+
-
improvement of propane-1,3-diol production by a novel propane-1,3-diol operon of three genes (dhaB1 and dhaB2 from Clostridium butyricum and YqhD from Escherichia coli) tandemly arrayed under the control of a constitutive, temperature-sensitive promoter in the vector pBV220 for heterologous expression in Escherichia coli
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-
?
3-hydroxypropanal + NADPH + H+
propane-1,3-diol + NADP+
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the Escherichia coli yqhD homolog can replace the function of DhaT in the Klebsiella pneumoniae AK mutant strain defective in 1,3-PD oxidoreductase activity (DhaT). The yqhD homolog restores propane-1,3-diol production and 1,3-PD oxidoreductase activity. Level of propane-1,3-diol production during batch fermentation in the recombinant strain is comparable to that of the parent strain
-
-
?
3-hydroxypropanal + NADPH + H+
propane-1,3-diol + NADP+
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improvement of propane-1,3-diol production by a novel propane-1,3-diol operon of three genes (dhaB1 and dhaB2 from Clostridium butyricum and YqhD from Escherichia coli) tandemly arrayed under the control of a constitutive, temperature-sensitive promoter in the vector pBV220 for heterologous expression in Escherichia coli
-
-
?
3-hydroxypropanal + NADPH + H+
propane-1,3-diol + NADP+
NADPH is not substrate for wild-type, but for mutant D41G
-
-
r
3-hydroxypropionaldehyde + NADH
propane-1,3-diol + NAD+
-
recombinant mutant Clostridium acetobutylicum strain DG1(pSPD5) expressing the enzyme from an introduced plasmid
-
-
?
3-hydroxypropionaldehyde + NADH
propane-1,3-diol + NAD+
-
recombinant mutant Clostridium acetobutylicum strain DG1(pSPD5) expressing the enzyme from an introduced plasmid
-
-
?
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
-
the enzyme is important in vivo for convertion of glycerol into propane-1,3-diol as second step after dehydration of glycerol by coenzyme B12-dependent glycerol dehydratase
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
24.1% activity compared to propane-1,3-diol
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
Clostridium butyricum YJH-09
-
24.1% activity compared to propane-1,3-diol
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
r
propane-1,2-diol + NAD+
2-hydroxypropanal + NADH + H+
-
21.5% activity compared to propane-1,3-diol
-
-
r
propane-1,2-diol + NAD+
2-hydroxypropanal + NADH + H+
Clostridium butyricum YJH-09
-
21.5% activity compared to propane-1,3-diol
-
-
r
propane-1,2-diol + NAD+
2-hydroxypropanal + NADH + H+
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
key enzyme of the 1,3-propanediol production pathway, high enzyme synthesis and activity in the anaerobic growth phase with increased use of glycerol
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
key enzyme of the 1,3-propanediol production pathway, high enzyme synthesis and activity in the anaerobic growth phase with increased use of glycerol
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
100% activity
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
Clostridium butyricum YJH-09
-
100% activity
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
r
additional information
?
-
-
the enzyme can also use 1,4-butanediol, 1-butyl alcohol, 1-propanol, glycerol, or 1,2-propylene glycol as substrate. The optimal substrate is 3-hydroxypropanal in the catalytic reduction reaction, and the optimal substrate is propane-1,3-diol in the catalytic oxidation reaction
-
-
?
additional information
?
-
-
the enzyme cannot oxidize 1-butanol, 1-propanol, and ethanol
-
-
-
additional information
?
-
-
the enzyme can also use 1,4-butanediol, 1-butyl alcohol, 1-propanol, glycerol, or 1,2-propylene glycol as substrate. The optimal substrate is 3-hydroxypropanal in the catalytic reduction reaction, and the optimal substrate is propane-1,3-diol in the catalytic oxidation reaction
-
-
?
additional information
?
-
Clostridium butyricum YJH-09
-
the enzyme cannot oxidize 1-butanol, 1-propanol, and ethanol
-
-
-
additional information
?
-
-
the enzyme can also use 1,4-butanediol, 1-butyl alcohol, 1-propanol, glycerol, or 1,2-propylene glycol as substrate. The optimal substrate is 3-hydroxypropanal in the catalytic reduction reaction, and the optimal substrate is propane-1,3-diol in the catalytic oxidation reaction
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity, PDOR can help reduce a broad range of aldehydes and ketones including 3-HPA, propionaldehyde, glyceraldehyde, acetone, hydroxyacetone, and dihydroxyacetone. No activity with acrolein. PDOR can also help oxidize many kinds of alcohols to generate the corresponding aldehydes, and this enzyme is most active with diols containing two primary hydroxy groups separated by one or two carbon atoms. Structure modeling, overview
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity, PDOR can help reduce a broad range of aldehydes and ketones including 3-HPA, propionaldehyde, glyceraldehyde, acetone, hydroxyacetone, and dihydroxyacetone. No activity with acrolein. PDOR can also help oxidize many kinds of alcohols to generate the corresponding aldehydes, and this enzyme is most active with diols containing two primary hydroxy groups separated by one or two carbon atoms. Structure modeling, overview
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity, PDOR can help reduce a broad range of aldehydes and ketones including 3-HPA, propionaldehyde, glyceraldehyde, acetone, hydroxyacetone, and dihydroxyacetone. No activity with acrolein. PDOR can also help oxidize many kinds of alcohols to generate the corresponding aldehydes, and this enzyme is most active with diols containing two primary hydroxy groups separated by one or two carbon atoms. Structure modeling, overview
-
-
?
additional information
?
-
enzyme additionally accepts ethanol, 1-propanol, 2-mercaptoethanol and their reduces their corresponding aldehydes. No substrates: methanol, 1-butanol, glycerol or 2-propanol
-
-
?
additional information
?
-
-
enzyme additionally accepts ethanol, 1-propanol, 2-mercaptoethanol and their reduces their corresponding aldehydes. No substrates: methanol, 1-butanol, glycerol or 2-propanol
-
-
?
additional information
?
-
enzyme additionally accepts ethanol, 1-propanol, 2-mercaptoethanol and their reduces their corresponding aldehydes. No substrates: methanol, 1-butanol, glycerol or 2-propanol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
part of the conversion of glycerol to 1,3-propanediol, not the limiting step
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
3-hydroxypropionaldehyde is an inhibitory intermediary metabolite in the 1,3-propanediol synthesis pathway during fermentation of raw material required for the synthesis of polytrimethylene terephthalate and other polyester fibers, accumulation of 3-hydroxypropanal in broth causes an irreversible cessation of the fermentation process
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
a key enzyme in the reductive pathway of anaerobic glycerol dissimilation converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
under physiological conditions, DhaT mostly catalyzes the forward reaction
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
under physiological conditions, DhaT mostly catalyzes the forward reaction
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
3-hydroxypropionaldehyde is an inhibitory intermediary metabolite in the 1,3-propanediol synthesis pathway during fermentation of raw material required for the synthesis of polytrimethylene terephthalate and other polyester fibers, accumulation of 3-hydroxypropanal in broth causes an irreversible cessation of the fermentation process
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction
-
-
r
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
-
the enzyme is important in vivo for convertion of glycerol into propane-1,3-diol as second step after dehydration of glycerol by coenzyme B12-dependent glycerol dehydratase
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
key enzyme of the 1,3-propanediol production pathway, high enzyme synthesis and activity in the anaerobic growth phase with increased use of glycerol
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
key enzyme of the 1,3-propanediol production pathway, high enzyme synthesis and activity in the anaerobic growth phase with increased use of glycerol
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
r
additional information
?
-
-
the enzyme can also use 1,4-butanediol, 1-butyl alcohol, 1-propanol, glycerol, or 1,2-propylene glycol as substrate. The optimal substrate is 3-hydroxypropanal in the catalytic reduction reaction, and the optimal substrate is propane-1,3-diol in the catalytic oxidation reaction
-
-
?
additional information
?
-
-
the enzyme can also use 1,4-butanediol, 1-butyl alcohol, 1-propanol, glycerol, or 1,2-propylene glycol as substrate. The optimal substrate is 3-hydroxypropanal in the catalytic reduction reaction, and the optimal substrate is propane-1,3-diol in the catalytic oxidation reaction
-
-
?
additional information
?
-
-
the enzyme can also use 1,4-butanediol, 1-butyl alcohol, 1-propanol, glycerol, or 1,2-propylene glycol as substrate. The optimal substrate is 3-hydroxypropanal in the catalytic reduction reaction, and the optimal substrate is propane-1,3-diol in the catalytic oxidation reaction
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the enzyme contains a cofactor motif, the conserved sequence G-GG-S-X-X-D. The binding site for cofactor NAD(H) is located in the deep hydrophilic pocket between the PDOR two domains
NADH
-
-
NADH
-
overexpression of PDOR leads to enhanced NADH and production ratio of NADH/NAD+ exceeds after the inducement of isopropyl-beta-D-thiogalactoside for the constructed strain
NADH
the electrostatic energy is the major force discriminating NADH from NADPH. Residue Asp41 is the key residue responsible for the coenzyme specificity
NADH
-
the enzyme prefers NADH to NAD+ as cofactor. 0.5 mM NADH is chosen as optimum concentration
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
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
K+
Li+
Mg2+
Mn2+
Na+
Ni2+
located near active site, crystallization data. The activity with 1,3-propanediol is highly dependent on the presence of Ni2+
additional information
Fe2+
activates to 150% at 5 mM, the enzyme contains two Fe2+-binding motifs, amino acid residues Asp189, Gln193, His258, and His272, are involved in the Fe2+ binding
additional information
-
the highest enzyme activity occurs with Mn2+, while the enzyme activity declines by 60-90% with other cations
additional information
-
the highest enzyme activity occurs with Mn2+, while the enzyme activity declines by 60-90% with other cations
additional information
no effects by NaCl, NH4Cl, and MgCl2 at 1 mM
additional information
addition of Co2+, Ni2+, or Mg2+ do not significantly affect PDOR activity at 5 mM
additional information
-
addition of Co2+, Ni2+, or Mg2+ do not significantly affect PDOR activity at 5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
imidazole
activity is reduced down to 32% in the presence of 1 mM imidazole and addition of 250 mM results in complete inactivity
EDTA
50 mM is necessary to obtain a 50% inhibition of enzymatic activity
additional information
-
in LB media, almost no activity of PDOR in Klebsiella pneumoniae ACCC10082, while it is higher in fermentation medium
-
additional information
-
when the concentration of 3-hydroxypropanal increases to a higher level in medium (ac 10 mmol/L), the activity of 1,3-propanediol oxidoreductase in cell decreases correspondingly, which leads to decrease of the 3-hydroxypropanal conversion rate, then the 3-hydroxypropanal concentration increasing is accelerated furthermore
-
additional information
poor effects by LiCl, DTT and sodium bisulfite at 1 mM
-
additional information
-
with 100 mM Na+, Li+, Mg2+ or NH4+ in addition to K+: 13-23% decrease in activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fumarate
-
25% activation of the enzyme, enhances the production of 1,3-propanediol from glycerol and the glycerol consumption in vivo
isopropyl-beta-D-thiogalactoside
-
inducer of gene expression, results in the increased activity of PDOR in LB medium
isopropyl-D-thiogalactoside
-
DhaT activity in the AK strain harboring pBR-dhaT-orfWX remarkably increases in the presence of isopropyl-D-thiogalactoside, although the activity is not proportional to the concentration of the inducer
-
additional information
poor effects by EDTA, 2-mercaptoethanol, and sodium carbazide
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.9
3-hydroxypropanal
pH and temperature not specified in the publication
0.107
NAD+
-
with propane-1,3-diol as cosubstrate, at pH 11.0 and 30°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
mathematical description and modelling of reaction and reaction kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.2
-
recombinant enzyme in Clostridium acetobutylicum mutant strain DG1
1.7
1.9
13.1
purified recombinant His-tagged enzyme, substrate propane-1,3-diol, pH 9.0, 55°C
13.7
crude cell extract with recombinant His-tagged enzyme, substrate 3-hydroxypropanal, pH 7.0, 37°C
32.6
purified recombinant His-tagged enzyme, substrate propane-1,3-diol, pH 9.5, 25°C
37
4.51
52.7
purified recombinant His-tagged enzyme, substrate 3-hydroxypropanal, pH 7.5, 37°C
89.7
purified recombinant His-tagged enzyme, substrate 3-hydroxypropanal, pH 7.0, 37°C
additional information
-
nucleotide pools of wild-type Clostridium butyricum strain VPI 3266 and recombinant Clostridium acetobutylicum mutant strain DG1
1.9
crude cell extract with recombinant His-tagged enzyme, substrate propane-1,3-diol, pH 9.0, 55°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
activity range, aldehyde reduction, profile overview
7 - 8.5
more than 80% of maximum activity for reduction of aldehyde
8 - 10.5
activity range, alcohol oxidation, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 40
activity range, aldehyde reduction, profile overview
25 - 45
activity range, alcohol oxidation, profile overview
30 - 55
over 80% of maximal activity within this range, aldehyde reduction, profile overview
30 - 65
over 60% of maximal activity within this range, alcohol oxidation, profile overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
the enzyme belongs to the type III alcohol dehydrogenases
evolution
-
the enzyme belongs to the type III alcohol dehydrogenases
-
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
-
evolution
-
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
-
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-HPA 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
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
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
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
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
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
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
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
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
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
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
-
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
-
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
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
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
-
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
-
metabolism
-
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
-
physiological function
-
growth behaviour on glucose is comparable between the wild type and a mutant strain lacking ORF lr0030. On glucose plus glycerol, the exponential growth rate of the lr_0030 mutant is lower compared to the wild type. Glycerol addition results in decreased ethanol production in the wild type, but not in lr_0030 mutant. Activity measurements using 3-hydrxypropanal as a substrate reveal lower activity of lr_0030 mutant extracts from exponential growing cells compared to wild type. During biotechnological 3-hydroxypropanal production using non-growing cells, the ratio 3-hydroxypropanal to 1,3-propanediol is approximately 7 in the wild type and lr_0030 mutant
physiological function
-
growth behaviour on glucose is comparable between the wild type and a ORF lr1734 deletion mutant. On glucose + glycerol, the exponential growth rate of the wild type and the deletion mutant are similar. Glycerol addition results in decreased ethanol production both in the wild type and mutant. During biotechnological 3-hydroxypropanal production using non-growing cells, the ratio 3-hydroxypropanal to 1,3-propanediol is approximately 7 in the wild type, whereas this ratio is 12.5 in the mutant lacking lr_1734
physiological function
Klebsiella pneumoniae converts 3 hydroxypropionaldehyde (3-HPA) to 1,3-propanediol (1,3-PD) during microbial production of 1,3-PD from glycerol
physiological function
-
Klebsiella pneumoniae converts 3 hydroxypropionaldehyde (3-HPA) to 1,3-propanediol (1,3-PD) during microbial production of 1,3-PD from glycerol
-
additional information
enzyme homology modeling and docking studies
additional information
the active site of PDOR is composed of the following amino acid residues, Asp32, Gly92, Gly93, Ser94, Thr134, Thr135, Thr138, Val146, Lys155, Leu177, Asp189, Leu182, Gln193, His258, and His272, which include the binding sites of Fe2+ and the cofactor NAD(H)
additional information
-
the active site of PDOR is composed of the following amino acid residues, Asp32, Gly92, Gly93, Ser94, Thr134, Thr135, Thr138, Val146, Lys155, Leu177, Asp189, Leu182, Gln193, His258, and His272, which include the binding sites of Fe2+ and the cofactor NAD(H)
additional information
-
the active site of PDOR is composed of the following amino acid residues, Asp32, Gly92, Gly93, Ser94, Thr134, Thr135, Thr138, Val146, Lys155, Leu177, Asp189, Leu182, Gln193, His258, and His272, which include the binding sites of Fe2+ and the cofactor NAD(H)
-
Show AA Sequence and Transmembrane Helices (1081 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
355000
384200
42000
42200
2 * 42200, calculated, 2 * 43000, SDS-PAGE of recombinant His-tagged protein
43000
43400
440000
446000
dynamic light scattering analysis of the purified protein in solution
46000
43000
2 * 42200, calculated, 2 * 43000, SDS-PAGE of recombinant His-tagged protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodecamer
10 * 42927, sequence calculation, 10 * 43000, recombinant His6-tagged enzyme, SDS-PAGE
octamer
oligomer
additional information
?
x * 42500, recombinant His-tagged enzyme, SDS-PAGE, x * 41993, sequence calculation
?
-
x * 42500, recombinant His-tagged enzyme, SDS-PAGE, x * 41993, sequence calculation
-
dimer
2 * 42200, calculated, 2 * 43000, SDS-PAGE of recombinant His-tagged protein
dimer
-
2 * 42200, calculated, 2 * 43000, SDS-PAGE of recombinant His-tagged protein
-
additional information
determination of secondary enzyme structure, 3D-modeling
additional information
-
determination of secondary enzyme structure, 3D-modeling
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by vapor diffusion in sitting drops at 20°C, at 2.7 A resolution. The enzyme shows a decameric structure, formed by a pentamer of dimers, which is the catalytic form of the enzyme. Dimers are associated by strong ionic interactions that are responsible for the highly stable in vivo packing of the enzyme. The decameric arrangement is related to the cooperativity between monomers
purified recombinant His-tagged enzyme, sitting-drop vapour diffusion, 22°C, 0.0015 ml of 55 mg/ml protein in 50 mM HEPES, pH 7.4, 150 mM NaCl, 1 mM MnCl2 and 2 mM DTT, is mixed with an equal volume of reservoir solution containing 0.1 M MES, pH 6.5, with 12% w/v PEG 20000, and 10 mM CaCl2, 8-24 h, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
to 3.2 A resolution. The electron density map around the active site shows no sign of a bound co-factor, but the active site metal could be located and identified as Ni2+
purified recombinant His-tagged protein in 20 mM Tris, pH 7.9, 150 mM NaCl, 0.25 mM TCEP, by nandroplet vapour diffusion method, cyrstallization buffer contains 20% PEG 300, 5% w/v PEG 8000, 10% glycerol, and 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis at 1.3 A resolution, modeling of 2 enzyme molecules, residues 1-359, complexed with 2 molecules of NADP+, 2 ions of Fe2+, 2 molecules of Tris, and 895 water molecules
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nore
D41A
mutation for relaxation of the coenzyme specificity, weakens the repulsion between Asp41 and the phosphate group esterified to the 2-hydroxyl group of the ribose at the adenine end of NADPH
D41G
mutation for relaxation of the coenzyme specificity, weakens the repulsion between Asp41 and the phosphate group esterified to the 2-hydroxyl group of the ribose at the adenine end of NADPH
additional information
nore
-
expression of the Clostridumm butyricum enzyme in Clostridium acetobutylicum strain DG1(pSPD5) leads to functional reduction of glycerol to 1,3-propanediol in a two-step process, the first step of glycerol reduction to 3-hydroxypropionaldehyde, which is then reduced to 1,3-propanediol, is performed by the B12-independent glycerol dehydratase
nore
-
expression of the Clostridumm butyricum enzyme in Clostridium acetobutylicum strain DG1(pSPD5) leads to functional reduction of glycerol to 1,3-propanediol in a two-step process, the first step of glycerol reduction to 3-hydroxypropionaldehyde, which is then reduced to 1,3-propanediol, is performed by the B12-independent glycerol dehydratase
-
additional information
engineering of a strain for optimized elimination of 3-hydroxypropionaldehyde, an inhibitory intermediary metabolite in the 1,3-propanediol synthesis pathway, from the broth during fermentation process of raw material required for the synthesis of polytrimethylene terephthalate and other polyester fibers, overview
additional information
-
engineering of a strain for optimized elimination of 3-hydroxypropionaldehyde, an inhibitory intermediary metabolite in the 1,3-propanediol synthesis pathway, from the broth during fermentation process of raw material required for the synthesis of polytrimethylene terephthalate and other polyester fibers, overview
additional information
-
Klebsiella pneumoniae AK mutant strain defective in 1,3-PD oxidoreductase activity (DhaT). The Escherichia coli yqhD homolog can replace the function of DhaT. The yqhD homolog restores propane-1,3-diol production and 1,3-PD oxidoreductase activity in the mutant Klebsiella pneumoniae strain defective in DhaT. Level of propane-1,3-diol production during batch fermentation in the recombinant strain is comparable to that of the parent strain
additional information
-
Klebsiella pneumoniae mutant strain AK (dhaD and dhaK replaced with the lacZ promoter-apramycin resistance gene cassette, such that the lacZ promoter is inserted in front of dhaB) and mutant strain AR (deletion of the dhaR gene and replaced with the lacZ promoter-apramycin resistance gene cassette, defective in the oxidative branch and in the reductive branch due to the loss of the dhaT and orfWX). propane-1,3-diol is still produced at lower level in the mutant strains, even though dhaT is removed, thus a a putative oxidoreductase may catalyze the production of propane-1,3-diol at lower level compared to DhaT. Dramatic increase in the production of propane-1,3-diol in the recombinant strains harboring the plasmid pBR-dhaT or pBR-dhaT-orfWX, which contain dhaT. Amount of propane-1,3-diol produced is lower in the AK and AR strain, which is harboring pBR-dhaT-orfWX (5.2 g/l), than the corresponding Cu, which is harboring pBR-dhaT-orfWX (7.7 g/l). During fermentation, the production yield is higher in the AK strain (0.57 mol/mol) than the Cu strain (0.47 mol/mol) harboring pBR-dhaT-orfWX
additional information
-
the PDOR isozyme activity increases 4.6times, when the yqhD gene is expressed in the Klebsiella pneumoniae mutant strains AK, which is a knockout mutant of the GDH and PDOR
additional information
-
Klebsiella pneumoniae mutant strain AK (dhaD and dhaK replaced with the lacZ promoter-apramycin resistance gene cassette, such that the lacZ promoter is inserted in front of dhaB) and mutant strain AR (deletion of the dhaR gene and replaced with the lacZ promoter-apramycin resistance gene cassette, defective in the oxidative branch and in the reductive branch due to the loss of the dhaT and orfWX). propane-1,3-diol is still produced at lower level in the mutant strains, even though dhaT is removed, thus a a putative oxidoreductase may catalyze the production of propane-1,3-diol at lower level compared to DhaT. Dramatic increase in the production of propane-1,3-diol in the recombinant strains harboring the plasmid pBR-dhaT or pBR-dhaT-orfWX, which contain dhaT. Amount of propane-1,3-diol produced is lower in the AK and AR strain, which is harboring pBR-dhaT-orfWX (5.2 g/l), than the corresponding Cu, which is harboring pBR-dhaT-orfWX (7.7 g/l). During fermentation, the production yield is higher in the AK strain (0.57 mol/mol) than the Cu strain (0.47 mol/mol) harboring pBR-dhaT-orfWX
-
additional information
-
the PDOR isozyme activity increases 4.6times, when the yqhD gene is expressed in the Klebsiella pneumoniae mutant strains AK, which is a knockout mutant of the GDH and PDOR
-
additional information
-
engineering of a strain for optimized elimination of 3-hydroxypropionaldehyde, an inhibitory intermediary metabolite in the 1,3-propanediol synthesis pathway, from the broth during fermentation process of raw material required for the synthesis of polytrimethylene terephthalate and other polyester fibers, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
purified recombinant His-tagged enzyme, 50% activityy remaining after 1 h and inactivation aafter 5 h at pH 6.0, 50% activity remaining after 3 h and 30% after 5 h at pH 7.5, inactivation after 1 h at pH 10.0
739886
additional information
additional information
PDOR is more stable in acid buffer than in alkaline condition
739886
additional information
-
PDOR is more stable in acid buffer than in alkaline condition
739886
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 45
purified recombinant His-tagged enzyme, 50% activity remaining after 3 h and 30% after 5 h at 30-37°C, inactivation after 2 h at 45°C
37
60% of enzyme relative activity remain after a 2h incubation at 37°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, Mn2+-DTT-HEPES buffer, stable for 3 days, 82% loss of activity after 3 weeks
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme 7.1-7.3fold from Escherichia coli strain JM109 by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant tagged selenomethionine-labeled enzyme from Escherichia coli by nickel affinity, ion exchange, and gel filtration chromatography and ultrafiltration
soluble recombinant His-tagged enzyme 6.6-6.7fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a synthetic pathway 1,3-propanediol production pathway is introduced in recombinant Escherichia coli consisting of glycerol dehydratase complex (dhaB123) and glycerol dehydratase reactivation factors (gdrAB) from Klebsiella pneumoniae and 1,3-propanediol oxidoreductase isoenzyme (yqhD) from Escherichia coli
all genes of the dha regulon, including the gene for 1,3-propanediol oxidoreductase of Klebsiella pneumoniae mobilized by the plasmid RP4:mini Mu and transferred to Escherichia coli
-
expression in Clostridium acetobutylicum mutant strain DG1 from plasmid pSPD5, subcloning in Escherichia coli
-
expression in Escherichia coli
gene dhaT, cloning from genomic DNA, DNA sequence determination, inducible high-level expression of the mostly soluble enzyme in Escherichia coli strain BL21(DE3)
-
gene dhaT, DNA and amino acid sequence determination and analysis, sequence comparisons
gene dhaT, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain JM109
gene dhaT, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in YqhD-deficient Escherichia coli strain BL21(DE3)
gene dhaT, expression of the N-terminally His-tagged in Escherichia coli strain BL21(DE3)
-
gene dhaT, high level co-expression of the 1,3-PD oxidoreductase with glycerol dehydratase, encoded by gene dhaB, and glycerol dehydratase reactivating factor, encoded by gene gdrAB, in Escherichia coli strain BL21 (DE3) using two incompatible plasmids, fed-batch fermentation of recombinant bacteria. The NADPH-linked alcohol dehydrogenase, which is encoded by yqhD, a gene from Escherichia coli, can non-specifically catalyze 3-hydroxypropionaldehyde converting to 1,3-propanediol with sufficient activity, overview
-
gene dhaT, part of the dha regulon, genetic structure, overview. Coexpressions of the PDOR and GDHt from gene dhaB in Klebsiella pneumoniae result in an increase of molar yield from 50.6-64.0% of 1,3-propanediol
-
gene dhaT, part of the dha regulon, genetic structure, recombinant expression in Escherichia coli
gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
gene dhaT, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene TM0920, expression of soluble N-terminally MGSDKIHHHHHH-tagged selenomethionine-labeled enzyme in Escherichia coli methionine auxotrophic strain DL41
genes for the production of propane-1,3-diol in Clostridium butyricum, dhaB1 and dhaB2, which encode the vitamin B12-independent glycerol dehydratase DhaB1 and its activating factor, DhaB2, respectively, tandemly arrayed with the Escherichia coli yqhD gene, which encodes the 1,3-propanediol oxidoreductase isoenzyme YqhD. Heterologous expression of the propane-1,3-diol operon under the control of the temperature-sensitive lambda phage PLPR promoter regulated by the cIts857 repressor, from plasmid pDY220, in Escherichia coli K-12 ER2925
-
overexpression of gene dhaT encoding PDOR (from vector pETPkan-dhaT) and transformed into Klebsiella pneumoniae
-
plasmid including Escherichia coli yqhD introduced into Klebsiella pneumoniae AK mutant strain defective in in 1,3-PD oxidoreductase activity (DhaT)
-
plasmids pUC18 K-dhaT and pUC18 K-gdh, carrying the genes dhaT encoding PDOR and gdh encoding glycerol dehydrogenase, respectively, transformed into a propane-1,3-diol native producer Klebsiella pneumoniae KG1
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recombinant plasmids containing dhaT expressed in Klebsiella pneumoniae Cu, and the mutant strains AK and AR
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the dhaD gene encoding glycerol dehydrogenase (GDH) and dhaT gene encoding 1,3-propanediol oxidoreductase (PDOR) inserted into pTD plasmid and overexpressed in Klebsiella pneumoniae ACCC 10082
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the dhaT gene coding for 1,3-PD dehydrogenase inserted into vector pET-YSBLIC and transformed into Escherichia coli BL21(DE3)
gene dhaT, part of the dha regulon, genetic structure, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, genetic structure, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, genetic structure, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
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gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in M1 medium containing 20 g/l glycerol and starch free fiberor xylan as supplement, the transcription level of the enzyme gene is 4.2-6.2 times higher than in glycerol alone and cellulose-supplemented glycerol
in M1 medium containing 20 g/l glycerol and starch free fiberor xylan as supplement, the transcription level of the enzyme gene is 4.2-6.2 times higher than in glycerol alone and cellulose-supplemented glycerol
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in M1 medium containing 20 g/l glycerol and starch free fiberor xylan as supplement, the transcription level of the enzyme gene is 4.2-6.2 times higher than in glycerol alone and cellulose-supplemented glycerol
Clostridium butyricum 15-42
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
synthesis
industry
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development of an economical and eco-friendly biological process for the production of propane-1,3-diol from renewable resources by construction of a novel operon including YqhD
industry
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development of an economical and eco-friendly biological process for the production of propane-1,3-diol from renewable resources by construction of a novel operon including YqhD
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synthesis
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Klebsiella pneumoniae is used for production of 1,3-propanediol by the enzyme which is utilized in plastic industry
synthesis
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the enzyme is useful in 1,3-propanediol production from glycerol, a byproduct in biodiesel production, by an enzymatic bioconversion in a membrane reactor in which the NAD+ coenzyme can be regenerated, mathematical description and modelling of the system, overview
synthesis
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constitutive overexpression of 1,3-PD oxidoreductase in Klebsiella pneumoniae leads to a nearly 3fold decrease in peak level of the intermediary metabolite 3-hydroxypropionaldehyde and an increase of 16.5% in yield of 1,3-propanediol with respect to the wild-type strain
synthesis
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expression of the yqhD gene, encoding 3-propanediol oxidoreductase isoenzyme from Escherichia coli and the dhaT gene, encoding 3-propanediol oxidoreductase from Klebsiella pneumoniae individually and concomitantly in Klebsiella pneumoniae using the double tac promoter expression plasmid pEtac-dhaT-tac-yqhD. The three resultant recombinant strains show that the peak values for 3-hydroxypropionaldehyde production in broth of the three recombinant strains are less than 25% of that of the parent strain. Expression of dhaT reduces formation of by-products ethanol and lactic acid and increases molar yield of 1,3-propanediol slightly, while expression of yqhD does not enhance molar yield of 1,3-propanediol, but increases ethanol concentration in broth as NADPH participation in transforming 3-hydroxypropionaldehyde to 1,3-propanediol allows more cellular NADH to be used to produce ethanol. Co-expression of both genes therefore decreases by-products and increases the molar yield of 1,3-propanediol by 11.8%, by catalyzing 3-hydroxypropionaldehyde conversion to 1,3-propanediol using the two cofactors NADH and NADPH
synthesis