Application | Comment | Organism |
---|---|---|
biofuel production | ethanol production by the hyperthermophilic archaeon Pyrococcus furiosus by expression of bacterial bifunctional alcohol dehydrogenase from Thermoanaerobacter sp. X514. Ethanol and acetate are the only major carbon end-products from glucose under these conditions. The amount of ethanol produced per estimated glucose consumed is increased from the background level 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Te-AdhEA) is still lower than that of the AAA pathway in Pyrococcus furiosus, which functions via the native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA) | Thermoanaerobacter sp. X514 |
biofuel production | expression in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted supports ethanol production. The highest amount of ethanol (estimated 61% theoretical yield) is produced when adhE and adhA from Thermoanaerobacter are co-expressed. A strain containing the Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is constructed. The AdhA gene is amplified from Thermoanaerobacter sp. X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514 is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of the bacterial strains expressing the various heterologous AdhE genes, only those containing AdhE and AdhA from Thermoanaerobacter sp. produced ethanol above background. The Thermoanaerobacter ethanolicus AdhEA strain containing both AdhE and AdhA produces the most ethanol (4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6 mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. For these four strains, the amount of ethanol produced per estimated glucose consumed is increased from the background level to 1.2, 1.0, 0.8 and 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Thermoanaerobacter ethanolicus AdhEA) is still lower than that of the previously reported AAA pathway in Pyrococcus furiosus, which functions via native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA) | Thermoanaerobacter ethanolicus |
Cloned (Comment) | Organism |
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expression in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted. A strain containing the Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is constructed. The AdhA gene is amplified from Thermoanaerobacter sp. X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514 is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of the bacterial strains expressing the various heterologous AdhE genes, only those containing AdhE and AdhA from Thermoanaerobacter sp. produced ethanol above background. The Thermoanaerobacter ethanolicus AdhEA strain containing both AdhE and AdhA produces the most ethanol (4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6 mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. For these four strains, the amount of ethanol produced per estimated glucose consumed is increased from the background level to 1.2, 1.0, 0.8 and 0.7 respectively | Thermoanaerobacter ethanolicus |
expression of the enzyme from Thermoanaerobacter sp. X514 in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted. Ethanol and acetate are the only major carbon end-products from glucose under these conditions. The amount of ethanol produced per estimated glucose consumed is increased from the background level 0.7 respectively | Thermoanaerobacter sp. X514 |
Protein Variants | Comment | Organism |
---|---|---|
additional information | expression of a mutant enzyme (with a glycine to aspartic acid mutation in the NADH binding site of the ADH domain of AdhE) in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted results in a reduced ethanol production to the background level | Thermoanaerobacter ethanolicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermoanaerobacter ethanolicus | C7IV28 | - |
- |
Thermoanaerobacter ethanolicus JW200 | C7IV28 | - |
- |
Thermoanaerobacter sp. X514 | B0K4A2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + NADH + H+ | AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities | Thermoanaerobacter sp. X514 | acetaldehyde + NAD+ + CoA | - |
? | |
acetyl-CoA + NADH + H+ | AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities | Thermoanaerobacter ethanolicus | acetaldehyde + NAD+ + CoA | - |
? | |
acetyl-CoA + NADH + H+ | AdhE is a bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities | Thermoanaerobacter ethanolicus JW200 | acetaldehyde + NAD+ + CoA | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AdhE | bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities | Thermoanaerobacter sp. X514 |
AdhE | bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities | Thermoanaerobacter ethanolicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Thermoanaerobacter sp. X514 | |
NADH | - |
Thermoanaerobacter ethanolicus |