EC Number | Application | Comment | Organism |
---|---|---|---|
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.22 | 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 | Bifidobacterium breve |
4.1.2.22 | Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase from Bifidobacterium adolescentis 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 |
4.1.2.22 | Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase from Bifidobacterium lactis 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 |
4.1.2.22 | Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase from Clostridium acetobutylicum 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 |
4.1.2.22 | Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase from Lactobacillus plantarum 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 |
4.1.2.22 | Saccharomyces cerevisiae does not demonstrate efficient phosphoketolase activity naturally. When phosphoketolase from Leuconostoc mesenteroides 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.2.9 | Bifidobacterium adolescentis | A0A0G9MEQ1 | - |
- |
4.1.2.9 | Bifidobacterium animalis subsp. lactis | AJD88698.1 | - |
- |
4.1.2.9 | Bifidobacterium breve | A0A0L0LT01 | - |
- |
4.1.2.9 | Clostridium acetobutylicum | KHD36088.1 | - |
- |
4.1.2.9 | Lactiplantibacillus plantarum | KRU18827.1 | - |
- |
4.1.2.9 | Lactiplantibacillus plantarum | KRU19755.1 | - |
- |
4.1.2.9 | Leuconostoc mesenteroides | Q5RLY5 | - |
- |
4.1.2.22 | Bifidobacterium adolescentis | A0A0G9MEQ1 | - |
- |
4.1.2.22 | Bifidobacterium animalis subsp. lactis | AJD88698.1 | - |
- |
4.1.2.22 | Bifidobacterium breve | A0A0L0LT01 | - |
- |
4.1.2.22 | Clostridium acetobutylicum | KHD36088.1 | - |
- |
4.1.2.22 | Lactiplantibacillus plantarum | KRU18827.1 | - |
- |
4.1.2.22 | Lactiplantibacillus plantarum | KRU19755.1 | - |
- |
4.1.2.22 | Leuconostoc mesenteroides | Q5RLY5 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.2.9 | 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 | - |
? | |
4.1.2.9 | 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 | - |
? | |
4.1.2.9 | 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 | - |
? | |
4.1.2.9 | 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 | - |
? | |
4.1.2.9 | D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows fructose-6-phosphate phosphoketolase activity | Leuconostoc mesenteroides | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
4.1.2.9 | D-Xylulose 5-phosphate + phosphate | the bifunctional enzyme also shows fructose-6-phosphate phosphoketolase activity | Bifidobacterium breve | Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
4.1.2.22 | D-Fructose 6-phosphate + phosphate | the bifunctional enzyme also shows activity with D-xylulose 5-phosphate (cf. EC 4.2.1.9) | Leuconostoc mesenteroides | Acetyl phosphate + D-erythrose 4-phosphate + H2O | - |
? | |
4.1.2.22 | D-Fructose 6-phosphate + phosphate | the bifunctional enzyme also shows activity with D-xylulose 5-phosphate (cf. EC 4.2.1.9) | Bifidobacterium breve | Acetyl phosphate + D-erythrose 4-phosphate + H2O | - |
? | |
4.1.2.22 | D-Fructose 6-phosphate + phosphate | the bifunctional enzyme also shows activity with D-xylulose 5-phosphate (cf. EC 4.2.1.9) | Bifidobacterium animalis subsp. lactis | Acetyl phosphate + D-erythrose 4-phosphate + H2O | - |
? | |
4.1.2.22 | D-Fructose 6-phosphate + phosphate | the bifunctional enzyme also shows activity with D-xylulose 5-phosphate (cf. EC 4.2.1.9) | Clostridium acetobutylicum | Acetyl phosphate + D-erythrose 4-phosphate + H2O | - |
? | |
4.1.2.22 | D-Fructose 6-phosphate + phosphate | the bifunctional enzyme also shows activity with D-xylulose 5-phosphate (cf. EC 4.2.1.9) | Lactiplantibacillus plantarum | Acetyl phosphate + D-erythrose 4-phosphate + H2O | - |
? | |
4.1.2.22 | D-Fructose 6-phosphate + phosphate | the bifunctional enzyme also shows activity with D-xylulose 5-phosphate (cf. EC 4.2.1.9) | Bifidobacterium adolescentis | Acetyl phosphate + D-erythrose 4-phosphate + H2O | - |
? |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.9 | 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 |
4.1.2.22 | metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism | Leuconostoc mesenteroides |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | 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 |
4.1.2.22 | metabolism | the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA-A key precursor in central carbon metabolism | Bifidobacterium adolescentis |