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Literature summary extracted from

  • Bergman, A.; Siewers, V.; Nielsen, J.; Chen, Y.
    Functional expression and evaluation of heterologous phosphoketolases in Saccharomyces cerevisiae (2016), AMB Express, 6, 115 .
    View publication on PubMedView publication on EuropePMC

Application

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

Cloned(Commentary)

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

Organism

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
-
-

Substrates and Products (Substrate)

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
-
 ?

General Information

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