Application | Comment | Organism |
---|---|---|
biotechnology | expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Leuconostoc mesenteroides |
biotechnology | expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Bifidobacterium breve |
biotechnology | expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Bifidobacterium animalis subsp. lactis |
biotechnology | expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Clostridium acetobutylicum |
biotechnology | expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Lactiplantibacillus plantarum |
biotechnology | expression of bacterial phosphoketolase in Saccharomyces cerevisiae (that does not demonstrate efficient phosphoketolase activity naturally) can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Bifidobacterium adolescentis |
Cloned (Comment) | Organism |
---|---|
Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase fome is expressed in Saccharomyces cerevisiae significant amounts of acetyl-phosphate are produced after provision of sugar phosphate substrates in vitro. Expression of bacterial phosphoketolase in Saccharomyces cerevisiae can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Leuconostoc mesenteroides |
Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase fome is expressed in Saccharomyces cerevisiae significant amounts of acetyl-phosphate are produced after provision of sugar phosphate substrates in vitro. Expression of bacterial phosphoketolase in Saccharomyces cerevisiae can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Lactiplantibacillus plantarum |
Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase is expressed in Saccharomyces cerevisiae significant amounts of acetyl-phosphate are produced after provision of sugar phosphate substrates in vitro. Expression of bacterial phosphoketolase in Saccharomyces cerevisiae can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Bifidobacterium animalis subsp. lactis |
Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase is expressed in Saccharomyces cerevisiae significant amounts of acetyl-phosphate are produced after provision of sugar phosphate substrates in vitro. Expression of bacterial phosphoketolase in Saccharomyces cerevisiae can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Clostridium acetobutylicum |
Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase is expressed in Saccharomyces cerevisiae significant amounts of acetyl-phosphate are produced after provision of sugar phosphate substrates in vitro. Expression of bacterial phosphoketolase in Saccharomyces cerevisiae can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Lactiplantibacillus plantarum |
Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase is expressed in Saccharomyces cerevisiae significant amounts of acetyl-phosphate are produced after provision of sugar phosphate substrates in vitro. Expression of bacterial phosphoketolase in Saccharomyces cerevisiae can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Bifidobacterium adolescentis |
Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When the phosphoketolase is expressed in Saccharomyces cerevisiae significant amounts of acetyl-phosphate are produced after provision of sugar phosphate substrates in vitro. Expression of bacterial phosphoketolase in Saccharomyces cerevisiae can efficiently divert intracellular carbon flux toward C2-synthesis, thus showing potential to be used in metabolic engineering strategies aimed to increase yields of acetyl-CoA derived compounds | Bifidobacterium breve |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bifidobacterium adolescentis | A0A0G9MEQ1 | - |
- |
Bifidobacterium animalis subsp. lactis | AJD88698.1 | - |
- |
Bifidobacterium breve | A0A0L0LT01 | - |
- |
Clostridium acetobutylicum | KHD36088.1 | - |
- |
Lactiplantibacillus plantarum | KRU18827.1 | - |
- |
Lactiplantibacillus plantarum | KRU19755.1 | - |
- |
Leuconostoc mesenteroides | Q5RLY5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity | Bifidobacterium animalis subsp. lactis | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity | Clostridium acetobutylicum | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity | Lactiplantibacillus plantarum | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity | Bifidobacterium adolescentis | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows fructose-6-phosphate phosphoketolase activity | Leuconostoc mesenteroides | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows fructose-6-phosphate phosphoketolase activity | Bifidobacterium breve | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism | Bifidobacterium breve |
metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism | Bifidobacterium animalis subsp. lactis |
metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism | Clostridium acetobutylicum |
metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism | Lactiplantibacillus plantarum |
metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism | Bifidobacterium adolescentis |
metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA-A key precursor in central carbon metabolism | Leuconostoc mesenteroides |
metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA-A key precursor in central carbon metabolism | Lactiplantibacillus plantarum |