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4.1.2.9: phosphoketolase

This is an abbreviated version!
For detailed information about phosphoketolase, go to the full flat file.

Word Map on EC 4.1.2.9

Reaction

D-xylulose 5-phosphate
+
phosphate
=
acetyl phosphate
 +
D-glyceraldehyde 3-phosphate
 +
H2O

Synonyms

CAC1343, D-xylulose 5-phosphate phosphoketolase, D-Xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase, D-Xylulose-5-phosphate phosphoketolase, FXPK, Pentulose-5-phosphate phosphoketolase, PhK, phosphoketolase, phosphoketolase-1, phosphoketolase-2, PKT, Pu5PPK, slr0453, X5P/F6P phosphoketolase, X5PPK, Xfp, XFPK, XPK, XpkA, xylulose-5-phosphate phosphoketolase, xylulose-5-phosphate/fructose-6-phosphate phosphoketolase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.9 phosphoketolase

Cloned

Cloned on EC 4.1.2.9 - phosphoketolase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in a prokaryotic vector, and the encoded protein is expressed in Escherichia coli
expressed in Corynebacterium glutamicum
expressed in Escherichia coli BL21 (DE3)
expressed in Escherichia coli BL21 (DE3) RIL cells
-
expressed in Escherichia coli BL21(DE3) RIL cells
-
expression in Corynebacterium glutamicum
-
expression in Escherichia coli
installation of a functional phosphoketolase pathway in xylose-fermenting Saccharomyces cerevisiae strain TMB3001c by heterologous expression of phosphotransacetylase and acetaldehyde dehydrogenase in combination with the native phosphoketolase
-
into the vector pET21a+ for expression in Escherichia coli BL21DE3 cells
into the vectors pET21a+ and pET28b+ for expression in Escherichia coli BL21DE3 cells
overexpression of the Bifidobacterium animalis xfp gene (encoding a phosphoketolase with dual substrate specificity) in a Corynebacterium glutamicum strain that is previously engineered to overproduce L-glutamic acid results in a 14% increase in the L-Glu yield from glucose
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
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
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