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1,2-propanediol + NAD+
2-hydroxypropanal + NADH
1,2-propylene glycol + NAD+
? + NADH + H+
1,3-propanediol + NAD+
3-hydroxypropanal + NADH
1,3-propanediol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
?
1,4-butanediol + NAD+
4-hydroxybutanal + NADH
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
1-butanol + NAD+
1-butanal + NADH + H+
-
-
-
r
1-butanol + NAD+
NADH + butanal
1-butyl alcohol + NAD+
1-butanal + NADH + H+
1-propanol + NAD+
1-propanal + NADH + H+
-
-
-
r
1-propanol + NAD+
NADH + propanal
1-propanol + NAD+
propanal + NADH + H+
2,3-butanediol + NAD+
? + NADH
-
-
-
-
r
2-butanol + NAD+
NADH + butanone
3-hydroxypropanal + NADH
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
3-hydroxypropanal + NADPH + H+
propane-1,3-diol + NADP+
3-hydroxypropionaldehyde + NADH
propane-1,3-diol + NAD+
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
acetaldehyde + NADH + H+
ethanol + NAD+
acetone + NADH + H+
?
-
25.3% activity compared to propionaldehyde
-
-
?
acetone + NADH + H+
? + NAD+
-
-
-
r
butyraldehyde + NADH + H+
butan-1-ol + NAD+
-
-
-
?
dihydroxyacetone + NADH + H+
? + NAD+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
ethanol + NAD+
NADH + ethanal
ethylene glycol + NAD+
NADH + ?
-
-
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
glyceraldehyde + NADH + H+
? + NAD+
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
glycerol + NAD+
glyceraldehyde + NADH + H+
glycerol + NADH
propane-1,3-diol + NAD+
hydroxyacetone + NADH + H+
?
-
30.6% activity compared to propionaldehyde
-
-
?
hydroxyacetone + NADH + H+
? + NAD+
-
-
-
r
propane-1,2-diol + NAD+
2-hydroxypropanal + NADH
-
-
-
-
r
propane-1,2-diol + NAD+
2-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+ + H+
3-hydroxypropanal + NADH
-
-
-
?
propane-1,3-diol + NADP+
3-hydroxypropanal + NADPH + H+
NADP+ is not substrate for wild-type, but for mutant D41G
-
-
r
propionaldehyde + NADH + H+
propan-1-ol + NAD+
valeraldehyde + NADH + H+
pentan-1-ol + NAD+
-
-
-
?
additional information
?
-
1,2-propanediol + NAD+
2-hydroxypropanal + NADH
-
-
-
?
1,2-propanediol + NAD+
2-hydroxypropanal + NADH
-
-
-
?
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
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
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH
-
-
-
-
?
1,4-butanediol + NAD+
4-hydroxybutanal + NADH
-
-
-
-
?
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1-butanol + NAD+
NADH + butanal
-
-
-
-
r
1-butanol + NAD+
NADH + butanal
-
-
-
-
?
1-butanol + NAD+
NADH + butanal
-
-
-
-
?
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
NADH + propanal
-
-
-
-
r
1-propanol + NAD+
NADH + propanal
-
-
-
-
?
1-propanol + NAD+
NADH + propanal
-
-
-
-
?
1-propanol + NAD+
NADH + propanal
-
-
-
-
?
1-propanol + NAD+
NADH + propanal
-
-
-
-
?
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
2-butanol + NAD+
NADH + butanone
-
-
-
-
?
2-butanol + NAD+
NADH + butanone
-
-
-
-
?
2-butanol + NAD+
NADH + butanone
-
-
-
-
?
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+
-
-
-
-
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+
-
-
-
-
?
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+
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
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
-
-
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 + 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
-
-
?
3-hydroxypropanal + NADPH + H+
propane-1,3-diol + NADP+
-
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+
-
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
propane-1,3-diol + NAD+
-
-
-
-
?
3-hydroxypropionaldehyde + NADH
propane-1,3-diol + NAD+
-
-
-
-
?
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
?
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
?
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
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
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
NADH + ethanal
-
-
-
-
r
ethanol + NAD+
NADH + ethanal
-
-
-
-
?
formaldehyde + NADH + H+
methanol + NAD+
-
-
-
?
formaldehyde + NADH + H+
methanol + NAD+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
24.1% activity compared to propane-1,3-diol
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
24.1% activity compared to propane-1,3-diol
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NADH
propane-1,3-diol + NAD+
-
-
-
-
?
glycerol + NADH
propane-1,3-diol + NAD+
-
-
-
-
?
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+
-
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
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
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
-
-
-
-
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
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
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
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+
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
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
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
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
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
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
-
r
propionaldehyde + NADH + H+
propan-1-ol + NAD+
-
100% activity
-
-
?
propionaldehyde + NADH + H+
propan-1-ol + NAD+
-
-
-
?
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-propylene glycol + NAD+
? + NADH + H+
1,3-propanediol + NAD+
3-hydroxypropanal + NADH + H+
-
-
-
?
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
1-butyl alcohol + NAD+
1-butanal + NADH + H+
1-propanol + NAD+
propanal + NADH + H+
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
3-hydroxypropionaldehyde + NADH
propane-1,3-diol + NAD+
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
glycerol + NAD+
glyceraldehyde + NADH + H+
glycerol + NADH
propane-1,3-diol + NAD+
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
additional information
?
-
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,2-propylene glycol + NAD+
? + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-butyl alcohol + NAD+
1-butanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
r
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
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+
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
propane-1,3-diol + NAD+
-
-
-
-
?
3-hydroxypropionaldehyde + NADH
propane-1,3-diol + NAD+
-
-
-
-
?
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
?
3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
-
-
-
-
?
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+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NADH
propane-1,3-diol + NAD+
-
-
-
-
?
glycerol + NADH
propane-1,3-diol + NAD+
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
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
-
-
-
-
?
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
-
-
-
-
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
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
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
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
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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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)
-
additional information
-
enzyme homology modeling and docking studies
-
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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
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expressed in Escherichia coli BL21 cells
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expression in Clostridium acetobutylicum mutant strain DG1 from plasmid pSPD5, subcloning in Escherichia coli
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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)
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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)
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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
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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
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overexpression in Escherichia coli
-
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)
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plasmid pUC18K-dhaT transformed into Klebsiella pneumoniae KG1
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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
-
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
-
the dhaT gene coding for 1,3-PD dehydrogenase inserted into vector pET-YSBLIC and transformed into Escherichia coli BL21(DE3)
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
gene dhaT, part of the dha regulon, genetic structure, recombinant expression in Escherichia coli
-
gene dhaT, part of the dha regulon, genetic structure, recombinant expression in Escherichia coli
-
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, part of the dha regulon, recombinant expression in Escherichia coli
-
gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
-
gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
-
gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
-
gene dhaT, part of the dha regulon, recombinant expression in Escherichia coli
-
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industry
-
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
-
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
-
synthesis
-
Klebsiella pneumoniae is used for production of 1,3-propanediol by the enzyme which is utilized in plastic industry
synthesis
-
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
-
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
-
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
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
genetic engineering of Klebsiella pneumoniae for production of 1.3-propanediol from glycerol. Constitutive expression of the dhaT gene alone gives the highest yield, fed-batch fermentation results in efficient production of 1,3-propanediol from either pure or crude glycerol, without by-product formation
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
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
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
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
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
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
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
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
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
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
synthesis
Escherichia coli is engineered to produce 1,3-propanediol from glycerol, an inexpensive carbon source. This is done by introducing a synthetic 1,3-propanediol production pathway 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. When 10 mM succinate is added to the medium, the titer of 1,3-propanediol and the glycerol consumption increase to 9.9 and 23.84 g/l, respectively. In addition, the ratio of NADH to NAD+ increases by 43%. Succinate addition is a promising route for the biotechnological production of NADH-dependent microbial metabolites
synthesis
NADH-dependent 1,3-propanediol oxidoreductase is a key enzyme for the production of 1,3-propanediol in soluble cell extract. Klebsiella pneumoniae J2B shows a high potential for the production of 1,3-propanediol from glycerol. Optimization of the culture conditions and the elimination of lactate synthesis improves 1,3-propanediol production significantly
synthesis
-
Klebsiella pneumoniae is used for production of 1,3-propanediol by the enzyme which is utilized in plastic industry
-
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
-
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
-
synthesis
-
NADH-dependent 1,3-propanediol oxidoreductase is a key enzyme for the production of 1,3-propanediol in soluble cell extract. Klebsiella pneumoniae J2B shows a high potential for the production of 1,3-propanediol from glycerol. Optimization of the culture conditions and the elimination of lactate synthesis improves 1,3-propanediol production significantly
-
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
-
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Johnson, E.A.; Lin, E.C.C.
Klebsiella pneumoniae 1,3-propanediol:NAD+ oxidoreductase
J. Bacteriol.
169
2050-2054
1987
Klebsiella pneumoniae
brenda
Heyndrickx, M.; De Vos, P.; Vancanneyt, M.; De Ley, J.
The fermentation of glycerol by Clostridium butyricum LMG 1212t2 and 1213t1 and C. pasteurianum LMG 3285
Appl. Microbiol. Biotechnol.
34
637-642
1991
Clostridium butyricum, Clostridium pasteurianum, Clostridium pasteurianum LMG 3285, Clostridium butyricum LMG 1212t2
-
brenda
Talarico, T.L.; Axelsson, L.T.; Novotny, J.; Fiuzat, M.; Dobrogosz, W.J.
Utilization of glycerol as a hydrogen acceptor by Lactobacillus reuteri: purification of 1,3-propanediol:NAD+ oxidoreductase
Appl. Environ. Microbiol.
56
943-948
1990
Limosilactobacillus reuteri
brenda
Abeles, R.H.; Brownstein, A.M.; Randles, C.H.
beta-Hydroxypropionaldehyde, an intermediate in the formation of 1,3-propanediol by Aerobacter aerogenes
Biochim. Biophys. Acta
41
530-531
1960
Klebsiella pneumoniae
brenda
Schutz, H.; Radler, F.
Anaerobic reduction of glycerol to propanediol-1,3 by Lactobacillus brevis and Lactobacillus buchneri
Syst. Appl. Microbiol.
5
169-178
1984
Levilactobacillus brevis, Lentilactobacillus buchneri
-
brenda
Sprenger, G.A.; Hammer, B.A.; Johnson, E.A.; Lin, E.C.C.
Anaerobic growth of Escherichia coli on glycerol by importing genes of the dha regulon from Klebsiella pneumoniae
J. Gen. Microbiol.
135
1255-1262
1989
Klebsiella pneumoniae
brenda
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
Luers, F.; Seyfried, M.; Daniel, R.; Gottschalk, G.
Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum: cloning and expression of the gene encoding 1,3-propanediol dehydrogenase
FEMS Microbiol. Lett.
154
337-345
1997
Clostridium pasteurianum
brenda
Malaoui, H.; Marczak, R.
Purification and characterization of the 1,3-propanediol dehydrogenase of Clostridium butyricum E5
Enzyme Microb. Technol.
27
399-405
2000
Clostridium butyricum, Clostridium butyricum E5
brenda
Abbad-Andaloussi, S.; Amine, J.; Gerard, P.; Petitdemange, H.
Effect of glucose on glycerol metabolism by Clostridium butyricum DSM 5431
J. Appl. Microbiol.
84
515-522
1998
Clostridium butyricum
brenda
Veiga-da-Cunha, M.; Foster, M.A.
1,3-Propanediol:NAD+ oxidoreductases of Lactobacillus brevis and Lactobacillus buchneri
Appl. Environ. Microbiol.
58
2005-2010
1992
Levilactobacillus brevis, Lentilactobacillus buchneri
brenda
Zheng, Y.; Yang, C.; Baishan, F.
Cloning and sequence analysis of the dhaT gene of the 1,3-propanediol regulon from Klebsiella pneumoniae
Biotechnol. Lett.
26
251-255
2004
Klebsiella pneumoniae (Q7WRJ3), Klebsiella pneumoniae
brenda
Schwarzenbacher, R.; von Delft, F.; Canaves, J.M.; Brinen, L.S.; Dai, X.; Deacon, A.M.; Elsliger, M.A.; Eshaghi, S.; Floyd, R.; Godzik, A.; Grittini, C.; Grzechnik, S.K.; Guda, C.; Jaroszewski, L.; Karlak, C.; Klock, H.E.; Koesema, E.; Kovarik, J.S.; Kreusch, A.; Kuhn, P.; Lesley, S.A.; McMullan, D.; McPhillips, T.M.; Miller, M.A.; Miller, M.D.; Morse, A.; Moy, K.; Ouyang, J.; Page, R.; Robb, A.; Rodrigues, K.; Selby, T.L.; Spraggon, G.; Stevens, R.C.; van den Bedem, H.; Velasquez, J.; Vincent, J.; Wang, X.; West, B.; Wolf, G.; Hodgson, K.O.; Wooley, J.; Wilson, I.A.
Crystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3 A resolution
Proteins
54
174-177
2003
Thermotoga maritima (Q9X022), Thermotoga maritima
brenda
Nemeth, A.; Kupcsulik, B.; Sevella, B.
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Klebsiella pneumoniae, Klebsiella pneumoniae DSM 2026
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Lin, R.; Liu, H.; Hao, J.; Cheng, K.; Liu, D.
Enhancement of 1,3-propanediol production by Klebsiella pneumoniae with fumarate addition
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Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
brenda
Gonzalez-Pajuelo, M.; Meynial-Salles, I.; Mendes, F.; Soucaille, P.; Vasconcelos, I.
Microbial conversion of glycerol to 1,3-propanediol: physiological comparison of a natural producer, Clostridium butyricum VPI 3266, and an engineered strain, Clostridium acetobutylicum DG1(pSPD5)
Appl. Environ. Microbiol.
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Clostridium butyricum, Clostridium butyricum VPI 3266
brenda
Fenghuan, W.; Huijin, Q.; He, H.; Tan, T.
High-level expression of the 1,3-propanediol oxidoreductase from Klebsiella pneumoniae in Escherichia coli
Mol. Biotechnol.
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Klebsiella pneumoniae
brenda
Wang, F.; Qu, H.; Zhang, D.; Tian, P.; Tan, T.
Production of 1,3-propanediol from glycerol by recombinant E. coli using incompatible plasmids system
Mol. Biotechnol.
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Klebsiella pneumoniae
brenda
Marcal, D.; Rego, A.T.; Fogg, M.J.; Wilson, K.S.; Carrondo, M.A.; Enguita, F.J.
Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
Acta Crystallogr. Sect. F
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249-251
2007
Klebsiella pneumoniae
brenda
Nemeth, A.; Sevella, B.
Development of a new bioprocess for production of 1,3-propanediol I.: modeling of glycerol bioconversion to 1,3-propanediol with Klebsiella pneumoniae enzymes
Appl. Biochem. Biotechnol.
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2008
Klebsiella pneumoniae
brenda
Hao, J.; Wang, W.; Tian, J.; Li, J.; Liu, D.
Decrease of 3-hydroxypropionaldehyde accumulation in 1,3-propanediol production by over-expressing dhaT gene in Klebsiella pneumoniae TUAC01
J. Ind. Microbiol. Biotechnol.
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Klebsiella pneumoniae (A3RL85), Klebsiella pneumoniae, Klebsiella pneumoniae TUAC01 (A3RL85), Klebsiella pneumoniae TUAC01
brenda
Ma, Z.; Rao, Z.; Zhuge, B.; Fang, H.; Liao, X.; Zhuge, J.
Construction of a Novel Expression System in Klebsiella pneumoniae and its Application for 1,3-Propanediol Production
Appl. Biochem. Biotechnol.
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2010
Klebsiella pneumoniae
brenda
Tang, X.; Tan, Y.; Zhu, H.; Zhao, K.; Shen, W.
Microbial conversion of glycerol to 1,3-propanediol by an engineered strain of Escherichia coli
Appl. Environ. Microbiol.
75
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Escherichia coli, Escherichia coli SYU 21132
brenda
Seo, M.Y.; Seo, J.W.; Heo, S.Y.; Baek, J.O.; Rairakhwada, D.; Oh, B.R.; Seo, P.S.; Choi, M.H.; Kim, C.H.
Elimination of by-product formation during production of propane-1,3-diol in Klebsiella pneumoniae by inactivation of glycerol oxidative pathway
Appl. Microbiol. Biotechnol.
84
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2009
Klebsiella pneumoniae, Klebsiella pneumoniae Cu
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Seo, J.W.; Seo, M.Y.; Oh, B.R.; Heo, S.Y.; Baek, J.O.; Rairakhwada, D.; Luo, L.H.; Hong, W.K.; Kim, C.H.
Identification and utilization of a 1,3-propanediol oxidoreductase isoenzyme for production of 1,3-propanediol from glycerol in Klebsiella pneumoniae
Appl. Microbiol. Biotechnol.
85
659-666
2009
Escherichia coli, Klebsiella pneumoniae
brenda
Zhao, L.; Zheng, Y.; Ma, X.; Wei, D.
Effects of over-expression of glycerol dehydrogenase and 1,3-propanediol oxidoreductase on bioconversion of glycerol into 1,3-propandediol by Klebsiella pneumoniae under micro-aerobic conditions
Bioprocess Biosyst. Eng.
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2009
Klebsiella pneumoniae
brenda
Chen, Z.; Liu, H.; Liu, D.
Regulation of 3-hydroxypropionaldehyde accumulation in Klebsiella pneumoniae by overexpression of dhaT and dhaD genes
Enzyme Microb. Technol.
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Klebsiella pneumoniae
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Marcal, D.; Rego, A.T.; Carrondo, M.A.; Enguita, F.J.
1,3-Propanediol dehydrogenase from Klebsiella pneumoniae: decameric quaternary structure and possible subunit cooperativity
J. Bacteriol.
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Klebsiella pneumoniae (Q7WRJ3), Klebsiella pneumoniae
brenda
Zhao, L.; Ma, X.; Zheng, Y.; Zhang, J.; Wei, G.; Wei, D.
Over-expression of glycerol dehydrogenase and 1,3-propanediol oxidoreductase in Klebsiella pneumoniae and their effects on conversion of glycerol into 1,3-propanediol in resting cell system
J. Chem. Technol. Biotechnol.
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Klebsiella pneumoniae
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brenda
Hao, J.; Lin, R.; Zheng, Z.; Sun, Y.; Liu, D.
3-Hydroxypropionaldehyde guided glycerol feeding strategy in aerobic 1,3-propanediol production by Klebsiella pneumoniae
J. Ind. Microbiol. Biotechnol.
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Klebsiella pneumoniae
brenda
Jeyakanthan, J.; Thamotharan, S.; Panjikar, S.; Kitamura, Y.; Nakagawa, N.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.
Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5
Acta Crystallogr. Sect. F
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2010
Aquifex aeolicus
brenda
Zhuge, B.; Zhang, C.; Fang, H.; Zhuge, J.; Permaul, K.
Expression of 1,3-propanediol oxidoreductase and its isoenzyme in Klebsiella pneumoniae for bioconversion of glycerol into 1,3-propanediol
Appl. Microbiol. Biotechnol.
87
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2010
Escherichia coli, Klebsiella pneumoniae (Q59477), Klebsiella pneumoniae
brenda
Ma, C.; Zhang, L.; Dai, J.; Xiu, Z.
Relaxing the coenzyme specificity of 1,3-propanediol oxidoreductase from Klebsiella pneumoniae by rational design
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Klebsiella pneumoniae (Q7WRJ3), Klebsiella pneumoniae
brenda
Elleuche, S.; Fodor, K.; Klippel, B.; von der Heyde, A.; Wilmanns, M.; Antranikian, G.
Structural and biochemical characterisation of a NAD+-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications
Appl. Microbiol. Biotechnol.
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8963-8975
2013
Oenococcus oeni (A0NIJ1), Oenococcus oeni, Oenococcus oeni ATCC BAA-1163 (A0NIJ1)
brenda
Oh, B.R.; Seo, J.W.; Heo, S.Y.; Luo, L.H.; Hong, W.K.; Park, D.H.; Kim, C.H.
Efficient production of 1,3-propanediol from glycerol upon constitutive expression of the 1,3-propanediol oxidoreductase gene in engineered Klebsiella pneumoniae with elimination of by-product formation
Bioprocess Biosyst. Eng.
36
757-763
2013
Klebsiella pneumoniae (Q59477), Klebsiella pneumoniae
brenda
Stevens, M.J.; Vollenweider, S.; Meile, L.; Lacroix, C.
1,3-Propanediol dehydrogenases in Lactobacillus reuteri: impact on central metabolism and 3-hydroxypropionaldehyde production
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Limosilactobacillus reuteri
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.
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2013
Citrobacter freundii (P45513), Citrobacter freundii
brenda
Qi, X.; Yun, J.; Qi, Y.; Zhang, H.; Wang, F.; Guo, Q.; Cao, Z.
Expression and characterization of a novel 1,3-propanediol dehydrogenase from Lactobacillus brevis
Appl. Biochem. Biotechnol.
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959-972
2016
Levilactobacillus brevis (A0A0C1Q6R1), Levilactobacillus brevis, Levilactobacillus brevis 6239 (A0A0C1Q6R1)
brenda
Jiang, W.; Wang, S.; Wang, Y.; Fang, B.
Key enzymes catalyzing glycerol to 1,3-propanediol
Biotechnol. Biofuels
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57
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Citrobacter freundii, Clostridium butyricum, Clostridium pasteurianum, Clostridium perfringens, Pantoea agglomerans, Klebsiella pneumoniae, Levilactobacillus brevis, Lentilactobacillus buchneri, Limosilactobacillus reuteri, Thermotoga maritima, Clostridium butyricum E5, Citrobacter freundii DSM 30040, Klebsiella pneumoniae DSM2026
brenda
Lama, S.; Ro, S.; Seol, E.; Sekar, B.; Ainala, S.; Thangappan, J.; Song, H.; Seung, D.; Park, S.
Characterization of 1,3-propanediol oxidoreductase (DhaT) from Klebsiella pneumoniae J2B
Biotechnol. Bioprocess Eng.
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971-979
2015
Klebsiella pneumoniae (Q59477), Klebsiella pneumoniae J2B (Q59477)
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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.
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2014
Citrobacter freundii (P45513)
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brenda
Durgapal, M.; Kumar, V.; Yang, T.H.; Lee, H.J.; Seung, D.; Park, S.
Production of 1,3-propanediol from glycerol using the newly isolated Klebsiella pneumoniae J2B
Bioresour. Technol.
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Klebsiella pneumoniae, Klebsiella pneumoniae (A7LGK0), Klebsiella pneumoniae J2B
brenda
Yun, J.; Yang, M.; Magocha, T.A.; Zhang, H.; Xue, Y.; Zhang, G.; Qi, X.; Sun, W.
Production of 1,3-propanediol using a novel 1,3-propanediol dehydrogenase from isolated Clostridium butyricum and co-biotransformation of whole cells
Biores. Technol.
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838-843
2018
Clostridium butyricum, Clostridium butyricum YJH-09
brenda
Apiwatanapiwat, W.; Vaithanomsat, P.; Thanapase, W.; Ratanakhanokchai, K.; Kosugi, A.
Xylan supplement improves 1,3-propanediol fermentation by Clostridium butyricum
J. Biosci. Bioeng.
125
662-668
2018
Clostridium butyricum, Clostridium butyricum 15-42
brenda