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
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4.1.2.9
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pentose
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xylose
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heterofermentative
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fructose-6-phosphate
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leuconostoc
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bifidobacteria
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phosphotransacetylase
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biotechnology
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embden-meyerhof-parnas
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heterolactic
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bifid
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synthesis
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xylulokinase
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acetylphosphate
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erythrose
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acetyl-coa-derived
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bifidobacteriaceae
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industry
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pharmacology
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biofuel production
- 4.1.2.9
- pentose
- xylose
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heterofermentative
- fructose-6-phosphate
- leuconostoc
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bifidobacteria
- phosphotransacetylase
- biotechnology
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embden-meyerhof-parnas
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heterolactic
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bifid
- synthesis
- xylulokinase
- acetylphosphate
- erythrose
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acetyl-coa-derived
- bifidobacteriaceae
- industry
- pharmacology
- biofuel production
Reaction
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
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Engineering on EC 4.1.2.9 - phosphoketolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
synthesis
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highest polyhydroxybutyrate production by Saccharomyces cerevisiae after 100 h is achieved with a strain harboring the phosphoketolase pathway, i.e xylulose-5-phosphate phosphoketolase EC 4.1.2.9 and acetate kinase EC 2.7.2.1 from Emericella nidulans and an acetyl-CoA synthetase variant L641P from Salmonella enterica on a single episomal plasmid to supply acetyl-CoA without the need of increased NADPH production by gapN integration
additional information
additional information
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since Lactobacillus plantarum has two phosphoketolase genes, xpk1 and xpk2, a delta xpk2 mutant is structured from Lactobacillus plantarum delta ldhL1-xpk1::tkt/pCU-PXylAB. Disruption of xpk2 causes a slight decrease in cell growth and fermentation rates, complete abolition of enzymes that have phosphoketolase activity, combined with introduction of enzymes that function as a bridge to the pentose phosphate pathway, enables homo-lactic acid production by pentose sugar fermentation
additional information
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the metabolic pathway in L-lactate dehydrogenase gene-deficient Lactobacillus plantarum NCIMB 8826 is engineered, redirection of the phosphoketolase pathway to the pentose phosphate pathway in Lactobacillus plantarum delta ldhL1 by substituting an endogenous phosphoketolase gene (xpk1) with the heterologous transketolase gene (tkt) from Lactococcus lactis IL 1403 is achieved, thereby shifts heterolactic acid fermentation to homolactic acid fermentation
additional information
Lactiplantibacillus plantarum NCIMB 8826
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the metabolic pathway in L-lactate dehydrogenase gene-deficient Lactobacillus plantarum NCIMB 8826 is engineered, redirection of the phosphoketolase pathway to the pentose phosphate pathway in Lactobacillus plantarum delta ldhL1 by substituting an endogenous phosphoketolase gene (xpk1) with the heterologous transketolase gene (tkt) from Lactococcus lactis IL 1403 is achieved, thereby shifts heterolactic acid fermentation to homolactic acid fermentation
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additional information
Lactiplantibacillus plantarum NCIMB 8826
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since Lactobacillus plantarum has two phosphoketolase genes, xpk1 and xpk2, a delta xpk2 mutant is structured from Lactobacillus plantarum delta ldhL1-xpk1::tkt/pCU-PXylAB. Disruption of xpk2 causes a slight decrease in cell growth and fermentation rates, complete abolition of enzymes that have phosphoketolase activity, combined with introduction of enzymes that function as a bridge to the pentose phosphate pathway, enables homo-lactic acid production by pentose sugar fermentation
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additional information
Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
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since Lactobacillus plantarum has two phosphoketolase genes, xpk1 and xpk2, a delta xpk2 mutant is structured from Lactobacillus plantarum delta ldhL1-xpk1::tkt/pCU-PXylAB. Disruption of xpk2 causes a slight decrease in cell growth and fermentation rates, complete abolition of enzymes that have phosphoketolase activity, combined with introduction of enzymes that function as a bridge to the pentose phosphate pathway, enables homo-lactic acid production by pentose sugar fermentation
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