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Literature summary for 4.1.2.9 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
Search for more literature for 4.1.2.9

Application

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(Commentary)

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

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
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Leuconostoc mesenteroides Q5RLY5
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-

Substrates and Products (Substrate)

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

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