1.1.1.202: 1,3-propanediol dehydrogenase
This is an abbreviated version!
For detailed information about 1,3-propanediol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.202
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1.1.1.202
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pneumoniae
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klebsiella
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dehydratase
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synthesis
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fed-batch
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butyricum
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freundii
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citrobacter
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3-hydroxypropionic
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dissimilation
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1,2-propanediol
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pasteurianum
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eutropha
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biodiesel
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reuteri
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industry
- 1.1.1.202
- pneumoniae
- klebsiella
- dehydratase
- synthesis
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fed-batch
- butyricum
- freundii
- citrobacter
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3-hydroxypropionic
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dissimilation
- 1,2-propanediol
- pasteurianum
-
eutropha
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biodiesel
- reuteri
- industry
Reaction
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, 1,3-propanediol-oxydoreductase, 1,3-propanediol:NAD oxidoreductase, 3-hydroxypropionaldehyde reductase, ADH3, dehydrogenase, 1,3-propanediol, DhaT, lr_0030, lr_1734, NADH-dependent 1,3-PD dehydrogenase, NADH-dependent 1,3-propanediol oxidoreductase, NADH-linked 1,3-propanediol oxidoreductase, PDOR, YqhD
ECTree
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Substrates Products
Substrates Products on EC 1.1.1.202 - 1,3-propanediol dehydrogenase
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REACTION DIAGRAM
acetone + NADH + H+
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25.3% activity compared to propionaldehyde
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hydroxyacetone + NADH + H+
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30.6% activity compared to propionaldehyde
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propane-1,3-diol + NADP+
3-hydroxypropanal + NADPH + H+
NADP+ is not substrate for wild-type, but for mutant D41G
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r
3-hydroxypropanal + NADH
activity with 1,3-propanediol is highly dependent on the presence of Ni2+
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1,3-propanediol + NAD+
3-hydroxypropanal + NADH
activity with 1,3-propanediol is highly dependent on the presence of Ni2+
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-
?
1,4-butanediol + NAD+
4-hydroxybutanal + NADH + H+
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-
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r
propane-1,3-diol + NAD+
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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
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3-hydroxypropanal + NADH
propane-1,3-diol + NAD+
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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
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3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
part of the conversion of glycerol to 1,3-propanediol, not the limiting step
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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
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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a key enzyme in the reductive pathway of anaerobic glycerol dissimilation converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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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%
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3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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in the cell exponential growth phase, the reaction catalyzed by 1,3-propanediol oxidoreductase is the rate limiting step in 1,3-propanediol production
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3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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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
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3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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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)
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3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
under physiological conditions, DhaT mostly catalyzes the forward reaction
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
under physiological conditions, DhaT mostly catalyzes the forward reaction
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
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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
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r
3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction
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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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3-hydroxypropanal + NADH + H+
propane-1,3-diol + NAD+
reduction of the aldehyde is the preferred reaction
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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
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
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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
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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
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?
3-hydroxypropanal + NADPH + H+
propane-1,3-diol + NADP+
NADPH is not substrate for wild-type, but for mutant D41G
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r
propane-1,3-diol + NAD+
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recombinant mutant Clostridium acetobutylicum strain DG1(pSPD5) expressing the enzyme from an introduced plasmid
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3-hydroxypropionaldehyde + NADH
propane-1,3-diol + NAD+
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recombinant mutant Clostridium acetobutylicum strain DG1(pSPD5) expressing the enzyme from an introduced plasmid
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3-hydroxypropionaldehyde + NADH + H+
propane-1,3-diol + NAD+
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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
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dihydroxyacetone + NADH + H+
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24.1% activity compared to propane-1,3-diol
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glycerol + NAD+
dihydroxyacetone + NADH + H+
Clostridium butyricum YJH-09
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24.1% activity compared to propane-1,3-diol
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r
glycerol + NAD+
dihydroxyacetone + NADH + H+
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2-hydroxypropanal + NADH + H+
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21.5% activity compared to propane-1,3-diol
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propane-1,2-diol + NAD+
2-hydroxypropanal + NADH + H+
Clostridium butyricum YJH-09
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21.5% activity compared to propane-1,3-diol
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propane-1,2-diol + NAD+
2-hydroxypropanal + NADH + H+
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propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
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key enzyme of the 1,3-propanediol production pathway, high enzyme synthesis and activity in the anaerobic growth phase with increased use of glycerol
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propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
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key enzyme of the 1,3-propanediol production pathway, high enzyme synthesis and activity in the anaerobic growth phase with increased use of glycerol
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propane-1,3-diol + NAD+
3-hydroxypropanal + NADH
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propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
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r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
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r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
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100% activity
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r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
Clostridium butyricum YJH-09
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100% activity
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r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
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r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
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r
propane-1,3-diol + NAD+
3-hydroxypropanal + NADH + H+
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r
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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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additional information
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the enzyme cannot oxidize 1-butanol, 1-propanol, and ethanol
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additional information
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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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additional information
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Clostridium butyricum YJH-09
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the enzyme cannot oxidize 1-butanol, 1-propanol, and ethanol
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additional information
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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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additional information
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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
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additional information
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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
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additional information
?
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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
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additional information
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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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additional information
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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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additional information
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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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