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D-fructose 6-phosphate + phosphate
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
D-xylulose 5-phosphate
pyruvate + acetyl phosphate
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
additional information
?
-
D-fructose 6-phosphate + phosphate
?
-
-
-
?
D-fructose 6-phosphate + phosphate
?
-
-
?
D-fructose 6-phosphate + phosphate
?
-
-
-
?
D-fructose 6-phosphate + phosphate
?
-
no reaction
-
-
?
D-fructose 6-phosphate + phosphate
?
-
-
-
-
?
D-fructose 6-phosphate + phosphate
?
-
-
-
?
D-fructose 6-phosphate + phosphate
?
-
-
-
-
?
D-fructose 6-phosphate + phosphate
?
-
-
-
-
?
D-fructose 6-phosphate + phosphate
?
-
no reaction
-
-
?
D-fructose 6-phosphate + phosphate
?
-
no reaction
-
-
?
D-fructose 6-phosphate + phosphate
?
-
no reaction
-
-
?
D-fructose 6-phosphate + phosphate
?
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
the enzyme has higher activity with D-xylulose 5-phosphate than D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
the specificity constant for D-xylulose 5-phosphate is significantly higher than that for D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
the enzyme has higher activity with D-xylulose 5-phosphate than D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
the specificity constant for D-xylulose 5-phosphate is significantly higher than that for D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
the bifunctional enzyme shows activity with fructose-6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for fructose-6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
-
the bifunctional enzyme shows activity with fructose-6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for fructose-6-phosphate
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
most specific substrate
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
-
most specific substrate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
ir
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
AJD88698.1
the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme also shows fructose-6-phosphate phosphoketolase activity
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
KHD36088.1
the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
Kluyveromyces phaseolosporus
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
Kluyveromyces phaseolosporus 108
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
KRU18827.1, KRU19755.1
the bifunctional enzyme also shows D-fructose 6-phosphate phosphoketolase activity
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
the specificity constant for D-xylulose 5-phosphate is significantly higher than that for D-fructose 6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
the specificity constant for D-xylulose 5-phosphate is significantly higher than that for D-fructose 6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for fructose-6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for fructose-6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme also shows fructose-6-phosphate phosphoketolase activity
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
the bifunctional enzyme shows activity with fructose-6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for fructose-6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
the bifunctional enzyme shows activity with fructose-6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for fructose-6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
the phosphoketolase pathway functions in heterofermentative bacteria where carbon flux through two sugar catabolic pathways to mixed acids (lactic acid and acetic acid) increases cellular ATP production. This pathway also serves as an alternative route to produce acetyl-CoA that bypasses the CO2 lost through pyruvate decarboxylation in the Embden-Meyerhof-Parnas pathway
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
the phosphoketolase pathway functions in heterofermentative bacteria where carbon flux through two sugar catabolic pathways to mixed acids (lactic acid and acetic acid) increases cellular ATP production. This pathway also serves as an alternative route to produce acetyl-CoA that bypasses the CO2 lost through pyruvate decarboxylation in the Embden-Meyerhof-Parnas pathway
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
the bifunctional enzyme shows activity with D-fructose 6-phosphate and D-xylulose 5-phosphate. It displays substantially higher preference for D-xylulose 5-phosphate than for D-fructose 6-phosphate
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
approximately the same activity as with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
approximately the same activity as with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
no activity
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
approximately the same activity as with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
approximately the same activity as with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
higher activity than with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
approximately the same activity as with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
about 50% of the activity with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
approximately the same activity as with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
higher activity than with D-xylulose 5-phosphate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
-
higher activity than with D-xylulose 5-phosphate
-
-
?
additional information
?
-
-
enzyme of the phosphoketolase pathway
-
?
additional information
?
-
-
enzyme is involved in pentose fermentation
-
-
?
additional information
?
-
-
enzyme of the pentose phosphate pathway
-
-
?
additional information
?
-
-
contribution of phosphoketolase to glucose catabolism is only slight
-
-
?
additional information
?
-
-
enzyme is involved in the pathway of glucose catabolism
-
-
?
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evolution
phylogenetic analysis of bacterial and fungal phosphoketolases, fungal phosphoketolases are of bacterial origin
malfunction
disruption of the putative phosphoketolase gene in wild-type Synechocystis leads to a deficiency in acetate production in the dark, indicative of a contribution of the phosphoketolase pathway to heterotrophic metabolism
metabolism
key enzyme in pentose metabolism
metabolism
lactic acid bacteria produce lactate, acetate, ethanol and carbon dioxide using the phosphoketolase pathway. When fructose is present, the redox balance can be maintained by the production of mannitol, which enables the formation of acetate instead of ethanol. The phosphoketolase has a lower energy yield in the form of ATP compared to that of the Embden-Meyerhof pathway (2 ATP for the Embden-Meyerhof pathway vs. only 1 for the phosphoketolase pathway) but it is used by lactic acid bacteria to ferment pentoses
metabolism
members from the order Bifidobacteriales differ from all other organisms in using a unique pathway for carbohydrate metabolism, known as the "bifid shunt", which utilizes the enzyme phosphoketolase to carry out the phosphorolysis of both fructose-6-phosphate and xylulose-5-phosphate. The existence of the bifid shunt allows bifidobacteria to produce more ATP from carbohydrates than through other conventional pathways. In contrast to bifidobacteria, the phosphoketolases found in other organisms (referred to XPK) are able to metabolize primarily xylulose-5-phosphate and show very little activity towards fructose-6-phosphate
metabolism
mutation of the gene encoding phosphoketolase almost completely abolishes flux through the pentose phosphoketolase pathway during growth on arabinose and results in decreased acetate/butyrate ratios
metabolism
the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism
metabolism
AJD88698.1
the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism
metabolism
KHD36088.1
the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism
metabolism
KRU18827.1, KRU19755.1
the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism
metabolism
the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA key precursor in central carbon metabolism
metabolism
the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA-A key precursor in central carbon metabolism
metabolism
KRU18827.1, KRU19755.1
the enzyme catalyzes the formation of acetyl-phosphate, which enzymatically can be converted into acetyl-CoA-A key precursor in central carbon metabolism
metabolism
the enzyme is indispensable for acetate production in the dark in all tested genetic backgrounds and nutrient conditions, which supports its physiological role as a phosphoketolase in the central carbon metabolism
metabolism
the enzyme is involved in pentose phosphoketolase pathway. This pathway has a primary role in arabinose metabolism of Clostridium acetobutylicum
metabolism
-
the phosphoketolase pathway functions in heterofermentative bacteria where carbon flux through two sugar catabolic pathways to mixed acids (lactic acid and acetic acid) increases cellular ATP production. This pathway also serves as an alternative route to produce acetyl-CoA that bypasses the CO2 lost through pyruvate decarboxylation in the Embden-Meyerhof-Parnas pathway
metabolism
the phosphoketolase route as a mechanism of acetyl-CoA synthesis provides an advantage to microbes whose carbon assimilation proceeds via de novo formation of the C-C bond. The draft analysis of the Methylomicrobium alcaliphilum genome reveals the open reading frames (ORFs) that encode a putative D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase (XFP, EC 4.1.2.9/EC 4.1.2.22) and acetate kinase (AcK, EC 2.7.2.1). The co-location of the xfp- and ack-like genes in the chromosome indicates that the phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z can represent a pathway for phosphosugars breakdown and an additional source of C2 compounds for acetyl-CoA synthesis
metabolism
-
lactic acid bacteria produce lactate, acetate, ethanol and carbon dioxide using the phosphoketolase pathway. When fructose is present, the redox balance can be maintained by the production of mannitol, which enables the formation of acetate instead of ethanol. The phosphoketolase has a lower energy yield in the form of ATP compared to that of the Embden-Meyerhof pathway (2 ATP for the Embden-Meyerhof pathway vs. only 1 for the phosphoketolase pathway) but it is used by lactic acid bacteria to ferment pentoses
-
metabolism
-
the phosphoketolase pathway functions in heterofermentative bacteria where carbon flux through two sugar catabolic pathways to mixed acids (lactic acid and acetic acid) increases cellular ATP production. This pathway also serves as an alternative route to produce acetyl-CoA that bypasses the CO2 lost through pyruvate decarboxylation in the Embden-Meyerhof-Parnas pathway
-
metabolism
-
lactic acid bacteria produce lactate, acetate, ethanol and carbon dioxide using the phosphoketolase pathway. When fructose is present, the redox balance can be maintained by the production of mannitol, which enables the formation of acetate instead of ethanol. The phosphoketolase has a lower energy yield in the form of ATP compared to that of the Embden-Meyerhof pathway (2 ATP for the Embden-Meyerhof pathway vs. only 1 for the phosphoketolase pathway) but it is used by lactic acid bacteria to ferment pentoses
-
metabolism
-
the phosphoketolase route as a mechanism of acetyl-CoA synthesis provides an advantage to microbes whose carbon assimilation proceeds via de novo formation of the C-C bond. The draft analysis of the Methylomicrobium alcaliphilum genome reveals the open reading frames (ORFs) that encode a putative D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase (XFP, EC 4.1.2.9/EC 4.1.2.22) and acetate kinase (AcK, EC 2.7.2.1). The co-location of the xfp- and ack-like genes in the chromosome indicates that the phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z can represent a pathway for phosphosugars breakdown and an additional source of C2 compounds for acetyl-CoA synthesis
-
physiological function
-
a phosphoketolase disruption mutant harboring the pXylRAB gene for catabolism of xylose lacks the phosphoketolase pathway and produces predominantly lactic acid from xylose via the pentose phosphate pathway, although its fermentation rate slightly decreases. Further introduction of the transketolase gene to disrupted phosphoketolase locus leads to restoration of the fermentation rate. As a result, the strain produces 50.1 g/l of L-lactic acid from xylose with a optical purity of 99.6% and a yield of 1.58 mol per mole xylose consumed
physiological function
the phosphoketolase pathway is active and contributes up to 40% of the xylose catabolic flux in Clostridium acetobutylicum. The split ratio of the phosphoketolase pathway to the pentose phosphate pathway is markedly increased when the xylose concentration in the culture medium is increased from 10 to 20 g per liter. A phosphoketolase-overexpressing strain shows slightly increased rates of cell growth and xylose consumption during the exponential growth phase. During the subsequent solventogenic phase, the phosphoketolase-overexpressing strain exhibits a strongly reduced xylose uptake rate and solvent yields and a high level of accumulation of acetate up to 75 mM. Unlike the control strain, the phosphoketolase-overexpressing strain does not reassimilate acetate at the solventogenic phase
physiological function
-
the phosphoketolase pathway is active and contributes up to 40% of the xylose catabolic flux in Clostridium acetobutylicum. The split ratio of the phosphoketolase pathway to the pentose phosphate pathway is markedly increased when the xylose concentration in the culture medium is increased from 10 to 20 g per liter. A phosphoketolase-overexpressing strain shows slightly increased rates of cell growth and xylose consumption during the exponential growth phase. During the subsequent solventogenic phase, the phosphoketolase-overexpressing strain exhibits a strongly reduced xylose uptake rate and solvent yields and a high level of accumulation of acetate up to 75 mM. Unlike the control strain, the phosphoketolase-overexpressing strain does not reassimilate acetate at the solventogenic phase
-
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Whitworth, D.A.; Ratledge, C.
Phosphoketolase in Rhodotorula graminis and other yeasts
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Candida sp. (in: Saccharomycetales), Vanrija humicola, Candida tropicalis, Rhodotorula glutinis, Rhodotorula graminis, Candida sp. (in: Saccharomycetales) 107
-
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Levels of enzymes of the pentose phosphate pathway in Pachysolen tannophilus Y-2460 and selected mutants
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Pachysolen tannophilus
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Properties of a pentulose-5-phosphate phosphoketolase from yeasts grown on xylose
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[Candida] boidinii, Cutaneotrichosporon curvatum, Debaryomyces hansenii, Yarrowia lipolytica, Lipomyces starkeyi, Pachysolen tannophilus, Priceomyces medius, Rhodotorula toruloides, Rhodotorula glutinis
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A novel pathway of glucose catabolism in Thiobacillus novellus
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no activity in Thiobacillus intermedius, no activity in Thiobacillus thioparus, Starkeya novella, Thiobacillus sp., Thiobacillus sp. A2
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Phosphoketolase
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Leuconostoc mesenteroides
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Pentose fermentation by Lactobacillus plantarum
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Lactiplantibacillus plantarum
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Saccharomyces cerevisiae, [Candida] boidinii, Cutaneotrichosporon curvatum, Kluyveromyces marxianus, Yarrowia lipolytica, Candida parapsilosis, Candida tropicalis, Cyberlindnera jadinii, Ogataea angusta, Cyberlindnera saturnus, Kluyveromyces phaseolosporus, Lipomyces starkeyi, Pachysolen tannophilus, Priceomyces medius, Rhodotorula toruloides, Rhodotorula glutinis, Cutaneotrichosporon cutaneum, Debaryomyces robertsiae, Ogataea angusta CBS 4732, Lipomyces starkeyi 1809, Candida parapsilosis NCYC 926, Pachysolen tannophilus 614, Kluyveromyces phaseolosporus 108, Ogataea angusta NCYC 495
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Fusarium oxysporum
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Expression of the xylulose 5-phosphate phosphoketolase gene, xpkA, from Lactobacillus pentosus MD363 is induced by sugars that are fermented via the phosphoketolase pathway and is repressed by glucose mediated by CcpA and the mannose phosphoenolpyruvate phosphotransferase system
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Phosphoketolase, a neglected enzyme of microbial carbohydrate metabolism
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Bifidobacterium animalis subsp. lactis
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Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis
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Metabolic engineering of a phosphoketolase pathway for pentose catabolism in Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Innovative metabolic pathway design for efficient l-glutamate production by suppressing CO2 emission
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Aspergillus nidulans, Saccharomyces cerevisiae, Penicillium chrysogenum, Aspergillus nidulans A187, Saccharomyces cerevisiae TMB3001, Penicillium chrysogenum WIS 54-1255
-
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Studies on the production of fungal polyketides in Aspergillus nidulans using systems biology tools
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brenda
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Cloning, expression, purification, cofactor requirements, and steady state kinetics of phosphoketolase-2 from Lactobacillus plantarum
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Lactiplantibacillus plantarum (Q88S87), Lactiplantibacillus plantarum (Q88U67), Lactiplantibacillus plantarum
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Systems analysis unfolds the relationship between the phosphoketolase pathway and growth in Aspergillus nidulans
PLoS ONE
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Aspergillus nidulans (Q5B3G7), Aspergillus nidulans
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Okano, K.; Yoshida, S.; Tanaka, T.; Ogino, C.; Fukuda, H.; Kondo, A.
Homo-D-lactic acid fermentation from arabinose by redirection of the phosphoketolase pathway to the pentose phosphate pathway in L-lactate dehydrogenase gene-deficient Lactobacillus plantarum
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Lactiplantibacillus plantarum, Lactiplantibacillus plantarum NCIMB 8826
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Improved production of homo-D-lactic acid via xylose fermentation by introduction of xylose assimilation genes and redirection of the phosphoketolase pathway to the pentose phosphate pathway in L-Lactate dehydrogenase gene-deficient Lactobacillus plantarum
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Lactiplantibacillus plantarum, Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
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A phosphoketolase Mpk1 of bacterial origin is adaptively required for full virulence in the insect-pathogenic fungus Metarhizium anisopliae
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Metarhizium anisopliae (C1K2N2), Metarhizium anisopliae
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Preliminary X-ray crystallographic analysis of the D-xylulose 5-phosphate phosphoketolase from Lactococcus lactis
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Lactococcus lactis, Lactococcus lactis IL 1403
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Lactiplantibacillus plantarum
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Lactococcus lactis
brenda
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Physiological characterization of recombinant Saccharomyces cerevisiae expressing the Aspergillus nidulans phosphoketolase pathway: validation of activity through 13C-based metabolic flux analysis
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Aspergillus nidulans
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Aspergillus nidulans
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Clostridium acetobutylicum (Q97JE3), Clostridium acetobutylicum, Clostridium acetobutylicum DSM 792 (Q97JE3)
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Clostridium acetobutylicum (Q97JE3), Clostridium acetobutylicum, Clostridium acetobutylicum DSM 792 (Q97JE3)
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Acetate kinase-an enzyme of the postulated phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z
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Petrareanu, G.; Balasu, M.; Vacaru, A.; Munteanu, C.; Ionescu, A.; Matei, I.; Szedlacsek, S.
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Termitomyces clypeatus (A0A023VSP0), Termitomyces clypeatus
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Phosphoketolase pathway engineering for carbon-efficient biocatalysis
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Bifidobacterium animalis subsp. lactis (Q9AEM9), Bifidobacterium animalis subsp. lactis DSM 101403 (Q9AEM9)
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702-710
2015
Limosilactobacillus reuteri (A0A0S4NL98), Limosilactobacillus reuteri (B3XLJ8), Limosilactobacillus reuteri, Limosilactobacillus reuteri DSM 200160 (B3XLJ8), Limosilactobacillus reuteri ATCC 53608 (A0A0S4NL98)
brenda
Henard, C.A.; Smith, H.K.; Guarnieri, M.T.
Phosphoketolase overexpression increases biomass and lipid yield from methane in an obligate methanotrophic biocatalyst
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152-158
2017
Methylotuvimicrobium buryatense, Methylotuvimicrobium buryatense 5GB1S
brenda
Sund, C.J.; Liu, S.; Germane, K.L.; Servinsky, M.D.; Gerlach, E.S.; Hurley, M.M.
Phosphoketolase flux in Clostridium acetobutylicum during growth on L-arabinose
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2015
Clostridium acetobutylicum (Q97JE3), Clostridium acetobutylicum
brenda
Xiong, W.; Lee, T.C.; Rommelfanger, S.; Gjersing, E.; Cano, M.; Maness, P.C.; Ghirardi, M.; Yu, J.
Phosphoketolase pathway contributes to carbon metabolism in cyanobacteria
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15187
2015
Synechocystis sp. PCC 6803 (P74690)
brenda
Gupta, R.S.; Nanda, A.; Khadka, B.
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Bifidobacterium longum (Q6R2Q7)
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Dele-Osibanjo, T.; Li, Q.; Zhang, X.; Guo, X.; Feng, J.; Liu, J.; Sun, X.; Wang, X.; Zhou, W.; Zheng, P.; Sun, J.; Ma, Y.
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103
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Bifidobacterium adolescentis
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