EC Number   |
General Information |
Reference |
|---|
   1.1.1.202 | 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 |
740927 |
| 1.1.1.202 | evolution |
PDOR belongs to the Fe-NAD-dependent alcohol dehydrogenase third family, and it is also a typical iron-ion activation-type dehydrogenase |
-, 740214 |
| 1.1.1.202 | evolution |
the enzyme belongs to the type III alcohol dehydrogenases |
-, 739886 |
| 1.1.1.202 | 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 |
740214 |
| 1.1.1.202 | 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 |
-, 740214 |
| 1.1.1.202 | 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 |
740927 |
| 1.1.1.202 | metabolism |
glycerol dehydratase, 1,3-propanediol dehydrogenase, and glycerol dehydrogenase are key enzymes in glycerol bioconversion into 1,3-propanediol and dihydroxyacetone |
-, 740214 |
| 1.1.1.202 | more |
enzyme homology modeling and docking studies |
-, 740216 |
| 1.1.1.202 | more |
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) |
-, 739886 |
| 1.1.1.202 | 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 |
725880 |
