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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General Information
General Information on EC 1.1.1.202 - 1,3-propanediol dehydrogenase
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evolution
malfunction
metabolism
physiological function
additional information
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
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PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
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PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
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PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
evolution
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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
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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
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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
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PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase
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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
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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
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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
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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
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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
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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
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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
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
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metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
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metabolism
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glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone
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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
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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
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Klebsiella pneumoniae converts 3 hydroxypropionaldehyde (3-HPA) to 1,3-propanediol (1,3-PD) during microbial production of 1,3-PD from glycerol
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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
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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
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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)
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