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Information on EC 4.1.2.9 - phosphoketolase
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4.1.2.9 phosphoketolaseIUBMB Comments
A thiamine-diphosphate protein.
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Word Map
- 4.1.2.9
- pentose
- xylose
-
heterofermentative
- fructose-6-phosphate
- leuconostoc
-
bifidobacteria
- phosphotransacetylase
- biotechnology
-
embden-meyerhof-parnas
-
heterolactic
-
bifid
- synthesis
- xylulokinase
- acetylphosphate
- erythrose
-
acetyl-coa-derived
- bifidobacteriaceae
- industry
- pharmacology
- biofuel production
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
phosphoketolase, phosphoketolase-2, d-xylulose 5-phosphate phosphoketolase, cac1343, xylulose-5-phosphate phosphoketolase, phosphoketolase-1, x5ppk, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAC1343
D-xylulose 5-phosphate phosphoketolase
D-Xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase
-
-
-
-
D-Xylulose-5-phosphate phosphoketolase
-
-
-
-
Pentulose-5-phosphate phosphoketolase
-
-
-
-
phosphoketolase
PKT
Pu5PPK
-
-
-
-
Xfp
XpkA
xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
phosphoketolase
Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
-
-
-
xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
-
-
xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
of an aldehyde, C-C bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (adding phosphate; acetyl-phosphate-forming)
A thiamine-diphosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY
9031-75-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Bifidobacterium animalis subsp. lactis DSM 101403
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
Bifidobacterium animalis subsp. lactis DSM 101403
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
Limosilactobacillus reuteri DSM 200160
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 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
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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
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additional information
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enzyme of the phosphoketolase pathway
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additional information
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enzyme is involved in pentose fermentation
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additional information
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enzyme of the pentose phosphate pathway
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additional information
?
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contribution of phosphoketolase to glucose catabolism is only slight
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additional information
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enzyme is involved in the pathway of glucose catabolism
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Crystal structures of phosphoketolase: thiamine diphosphate-dependent dehydration mechanism.
Dehydration
Sweet siblings with different faces: the mechanisms of FBP and F6P aldolase, transaldolase, transketolase and phosphoketolase revisited in light of recent structural data.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
D-fructofuranose 6-phosphate
apparent Km value, Mg2+
0.0004
D-fructose 6-phosphate
apparent Km value, Mn2+
0.16
D-fructose 6-phosphate
apparent Km value, Ca2+
9.84
D-fructose 6-phosphate
-
mutant T2A/I6T/H260Y, pH 6.5, 30°C
24
D-fructose 6-phosphate
D-fructose 6-phosphate and phosphate
3.6
D-xylulose 5-phosphate
xylulose 5-phosphate and phosphate
2.9
phosphate
D-fructose 6-phosphate and phosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.07
D-fructose 6-phosphate
-
mutant T2A/I6T/H260Y, pH 6.5, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
D-fructose 6-phosphate
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mutant T2A/I6T/H260Y, pH 6.5, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.052
purification step crude extract, histidine tail phosphoketolase-2
0.2
purification step Biogel P6 column, histidine tail phosphoketolase-2
0.61
purification step Sephacryl-300 column, histidine tail phosphoketolase-2
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7
5.5 - 7
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pH 5.5: about 50% of maximal activity, pH 7.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27.5 - 32.5
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27.5°C: about 70% of maximal activity, 32.5°C: about 30% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bi-functional xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
UniProt
brenda
bi-functional xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
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
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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
Limosilactobacillus reuteri DSM 200160
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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
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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
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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
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physiological function
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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
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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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Show AA Sequence and Transmembrane Helices (475 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 17% (w/v) PEG 3350 and 0.2 M NaSCN, at 18°C
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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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap Ni2+ metal affinity column chromatography and Superdex 200 gel filtration
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recombinant phosphoketolase-2 is purified using Ni-NTA resin, a Biogel P6 and a Sephacryl-300 column, in a second purification approach a DEAE-Sepharose and a Sephadex-300 column are used
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in a prokaryotic vector, and the encoded protein is expressed 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
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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
cloned in a prokaryotic vector, and the encoded protein is expressed in Escherichia coli
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cloned in a prokaryotic vector, and the encoded protein is expressed in Escherichia coli
cloned in a prokaryotic vector, and the encoded protein is expressed in Escherichia coli
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 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
KRU18827.1, KRU19755.1
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
AJD88698.1
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
KHD36088.1
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
KRU18827.1, KRU19755.1
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzymic activity is present in cells grown on arabinose but not glucose and mRNA expression is induced 185fold during growth on arabinose when compared to growth on glucose
the induction with different sugars indicates that the transcription of mpk1 can be upregulated by xylose, hexose sugars (glucose and galactose) or disaccharides (sucrose and trehalose) but not by mannitol, sorbose or sorbitol
enzymic activity is present in cells grown on arabinose but not glucose and mRNA expression is induced 185fold during growth on arabinose when compared to growth on glucose
enzymic activity is present in cells grown on arabinose but not glucose and mRNA expression is induced 185fold during growth on arabinose when compared to growth on glucose
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
biotechnology
industry
pharmacology
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polyketide natural products play an important role in the treatment of a wide range of human physiological disorders
synthesis
biofuel production
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overexpression of the PktB isoform leads to a 2fold increase in intracellular acetyl-CoA concentration, and a 2.6fold yield enhancement from methane to microbial biomass and lipids compared to wild-type, increasing the potential for methanotroph lipid-based fuel production
biofuel production
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overexpression of the PktB isoform leads to a 2fold increase in intracellular acetyl-CoA concentration, and a 2.6fold yield enhancement from methane to microbial biomass and lipids compared to wild-type, increasing the potential for methanotroph lipid-based fuel production
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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
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
biotechnology
AJD88698.1
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
biotechnology
KHD36088.1
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
biotechnology
KRU18827.1, KRU19755.1
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
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
biotechnology
pathway engineering advances in a high-potential alternative route, the phosphoketolase pathway, which facilitates bypass of pyruvate decarboxylation and enables complete carbon conservation in bioprocesses targeting pentose phosphate pathway and/or acetyl-CoA-derived products
biotechnology
Bifidobacterium animalis subsp. lactis DSM 101403
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pathway engineering advances in a high-potential alternative route, the phosphoketolase pathway, which facilitates bypass of pyruvate decarboxylation and enables complete carbon conservation in bioprocesses targeting pentose phosphate pathway and/or acetyl-CoA-derived products
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industry
-
the production of D-lactic acid as well as L-lactic acid is of significant importance for the practical application of polylactic acid, which is an important raw material for bioplastics that can be produced from biomass
industry
-
using the Lactobacillus plantarum NCIMB 8826 strain whose L-lactate dehydrogenase gene is deficient and whose phosphoketolase gene is substituted with a heterologous transketolase gene the fermentation of optically pure D-lactic acid from arabinose is achieved
industry
industrially important enzyme in the production of L-glutamic acid, mevalonate, isoprenoid precursors and isoprene
industry
Lactiplantibacillus plantarum NCIMB 8826
-
using the Lactobacillus plantarum NCIMB 8826 strain whose L-lactate dehydrogenase gene is deficient and whose phosphoketolase gene is substituted with a heterologous transketolase gene the fermentation of optically pure D-lactic acid from arabinose is achieved
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industry
Lactiplantibacillus plantarum NCIMB 8826
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the production of D-lactic acid as well as L-lactic acid is of significant importance for the practical application of polylactic acid, which is an important raw material for bioplastics that can be produced from biomass
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industry
Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
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the production of D-lactic acid as well as L-lactic acid is of significant importance for the practical application of polylactic acid, which is an important raw material for bioplastics that can be produced from biomass
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synthesis
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a phosphoketolase disruption mutant harboring the pXylRAB gene for catabolism of xylose lacks the phosphoketolasepathwas 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
synthesis
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metabolic engineering strategy to express the fungal genes of the phosphoketolase pathway in Saccharomyces cerevisiae. The utilization of the phosphoketolase pathway does not interfere with glucose assimilation through the Embden-Meyerhof-Parnas pathway and the expression of this route can contribute to increase the acetyl CoA supply
synthesis
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given that acetyl-CoA is a key intermediate in several biosynthetic pathways, phosphoketolase overexpression offers a viable strategy to enhance the economics of an array of biological methane conversion processes
synthesis
-
expression of mutant T2A/I6T/H260 in Corynebacterium glutamicum Z188 results in 16.67% and 18.19% improvement in L-glutamate titer and yield, respectively, compared with the wildtype
synthesis
-
given that acetyl-CoA is a key intermediate in several biosynthetic pathways, phosphoketolase overexpression offers a viable strategy to enhance the economics of an array of biological methane conversion processes
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Whitworth, D.A.; Ratledge, C.
Phosphoketolase in Rhodotorula graminis and other yeasts
J. Gen. Microbiol.
102
397-401
1977
Candida sp. (in: Saccharomycetales), Vanrija humicola, Candida tropicalis, Rhodotorula glutinis, Rhodotorula graminis, Candida sp. (in: Saccharomycetales) 107
-
brenda
Lachke, A.H.; Jeffries, T.W.
Levels of enzymes of the pentose phosphate pathway in Pachysolen tannophilus Y-2460 and selected mutants
Enzyme Microb. Technol.
8
353-359
1986
Pachysolen tannophilus
-
brenda
Ratledge, C.; Holdsworth, J.E.
Properties of a pentulose-5-phosphate phosphoketolase from yeasts grown on xylose
Appl. Microbiol. Biotechnol.
22
217-221
1985
[Candida] boidinii, Cutaneotrichosporon curvatum, Debaryomyces hansenii, Yarrowia lipolytica, Lipomyces starkeyi, Pachysolen tannophilus, Priceomyces medius, Rhodotorula toruloides, Rhodotorula glutinis
-
brenda
Greenley, D.E.; Smith, D.W.
A novel pathway of glucose catabolism in Thiobacillus novellus
Arch. Microbiol.
122
257-261
1979
no activity in Thiobacillus intermedius, no activity in Thiobacillus thioparus, Starkeya novella, Thiobacillus sp., Thiobacillus sp. A2
-
brenda
Goldberg, M.; Fessenden, J.M.; Racker, E.
Phosphoketolase
Methods Enzymol.
9
515-520
1966
Leuconostoc mesenteroides
-
brenda
Heath, E.C.; Hurwitz, J.; Horecker, B.L.; Ginsburg, A.
Pentose fermentation by Lactobacillus plantarum
J. Biol. Chem.
231
1009-1029
1958
Lactiplantibacillus plantarum
brenda
Evans, C.T.; Ratledge, C.
Induction of xylulose-5-phosphate phosphoketolase in a variety of yeasts grown on D-xylose: the key to efficient xylose metabolism
Arch. Microbiol.
139
48-52
1984
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
-
brenda
Matheron, C.; Delort, A.M.; Gaudet, G.; Forano, E.
Re-investigation of glucose metabolism in Fibrobacter succinogenes, using NMR spectroscopy and enzymatic assays. Evidence for pentose phosphates phosphoketolase and pyruvate formate lyase activities
Biochim. Biophys. Acta
1355
50-60
1997
Fibrobacter succinogenes, Fibrobacter intestinalis
brenda
Veiga-da Cunha, M.; Santos, H.; van Schaftingen, A.
Pathway and regulation of erythritol formation in Leuconostoc oenos
J. Bacteriol.
175
3941-3948
1993
Oenococcus oeni, Oenococcus oeni GM
brenda
Marounek, M.; Petr, O.
Fermentation of glucose and xylose in ruminal strains of Butyrivibrio fibrisolvens
Lett. Appl. Microbiol.
21
272-276
1995
Butyrivibrio fibrisolvens
brenda
Singh, A.
D-Xylose fermentation and catabolism in Fusarium oxysporum
Biochem. Int.
27
831-839
1992
Fusarium oxysporum
brenda
Posthuma, C.C.; Bader, R.; Engelmann, R.; Postma, P.W.; Hengstenberg, W.; Pouwels, P.H.
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
Appl. Environ. Microbiol.
68
831-837
2002
Lactiplantibacillus pentosus (Q937F6), Lactiplantibacillus pentosus, Lactiplantibacillus pentosus MD364 (Q937F6)
brenda
Rohr, L.M.; Teuber, M.; Meile, L.
Phosphoketolase, a neglected enzyme of microbial carbohydrate metabolism
Chimia
56
270-273
2002
Bifidobacterium animalis subsp. lactis
-
brenda
Meile, L.; Rohr, L.M.; Geissmann, T.A.; Herensperger, M.; Teuber, M.
Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis
J. Bacteriol.
183
2929-2936
2001
Bifidobacterium animalis subsp. lactis (Q9AEM9), Bifidobacterium animalis subsp. lactis
brenda
Sonderegger, M.; Schumperli, M.; Sauer, U.
Metabolic engineering of a phosphoketolase pathway for pentose catabolism in Saccharomyces cerevisiae
Appl. Environ. Microbiol.
70
2892-2897
2004
Saccharomyces cerevisiae
brenda
Arskoeld, E.; Lohmeier-Vogel, E.; Cao, R.; Roos, S.; Radstroem, P.; van Niel, E.W.
Phosphoketolase pathway dominates in Lactobacillus reuteri ATCC 55730 containing dual pathways for glycolysis
J. Bacteriol.
190
206-212
2008
Limosilactobacillus reuteri
brenda
Chinen, A.; Kozlov, Y.I.; Hara, Y.; Izui, H.; Yasueda, H.
Innovative metabolic pathway design for efficient l-glutamate production by suppressing CO2 emission
J. Biosci. Bioeng.
103
262-269
2007
Bifidobacterium animalis (A0PAD9), Bifidobacterium animalis, Bifidobacterium animalis JCM 1190 (A0PAD9)
brenda
Thykaer, J.; Nielsen, J.
Evidence, through C13-labelling analysis, of phosphoketolase activity in fungi
Process Biochem.
42
1050-1055
2007
Aspergillus nidulans, Saccharomyces cerevisiae, Penicillium chrysogenum, Aspergillus nidulans A187, Saccharomyces cerevisiae TMB3001, Penicillium chrysogenum WIS 54-1255
-
brenda
Panagiotou, G.; Andersen, M.R.; Grotkjaer, T.; Regueira, T.B.; Nielsen, J.; Olsson, L.
Studies on the production of fungal polyketides in Aspergillus nidulans using systems biology tools
Appl. Environ. Microbiol.
75
2212-2220
2009
Aspergillus nidulans
brenda
Yevenes, A.; Frey, P.A.
Cloning, expression, purification, cofactor requirements, and steady state kinetics of phosphoketolase-2 from Lactobacillus plantarum
Bioorg. Chem.
36
121-127
2008
Lactiplantibacillus plantarum (Q88S87), Lactiplantibacillus plantarum (Q88U67), Lactiplantibacillus plantarum
brenda
Panagiotou, G.; Andersen, M.R.; Grotkjaer, T.; Regueira, T.B.; Hofmann, G.; Nielsen, J.; Olsson, L.
Systems analysis unfolds the relationship between the phosphoketolase pathway and growth in Aspergillus nidulans
PLoS ONE
3
e3847
2008
Aspergillus nidulans (Q5B3G7), Aspergillus nidulans
brenda
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
Appl. Environ. Microbiol.
75
5175-5178
2009
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum NCIMB 8826
brenda
Okano, K.; Yoshida, S.; Yamada, R.; Tanaka, T.; Ogino, C.; Fukuda, H.; Kondo, A.
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
Appl. Environ. Microbiol.
75
7858-7861
2009
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
brenda
Duan, Z.; Shang, Y.; Gao, Q.; Zheng, P.; Wang, C.
A phosphoketolase Mpk1 of bacterial origin is adaptively required for full virulence in the insect-pathogenic fungus Metarhizium anisopliae
Environ. Microbiol.
11
2351-2360
2009
Metarhizium anisopliae (C1K2N2), Metarhizium anisopliae
brenda
Petrareanu, G.; Balasu, M.C.; Zander, U.; Scheidig, A.J.; Szedlacsek, S.E.
Preliminary X-ray crystallographic analysis of the D-xylulose 5-phosphate phosphoketolase from Lactococcus lactis
Acta Crystallogr. Sect. F
66
805-807
2010
Lactococcus lactis, Lactococcus lactis IL 1403
brenda
Sanchez, B.; Zuniga, M.; Gonzalez-Candelas, F.; de los Reyes-Gavilan, C.G.; Margolles, A.
Bacterial and eukaryotic phosphoketolases: phylogeny, distribution and evolution
J. Mol. Microbiol. Biotechnol.
18
37-51
2010
Lactiplantibacillus plantarum
brenda
Shinkawa, S.; Okano, K.; Yoshida, S.; Tanaka, T.; Ogino, C.; Fukuda, H.; Kondo, A.
Improved homo L-lactic acid fermentation from xylose by abolishment of the phosphoketolase pathway and enhancement of the pentose phosphate pathway in genetically modified xylose-assimilating Lactococcus lactis
Appl. Microbiol. Biotechnol.
91
1537-1544
2011
Lactococcus lactis
brenda
Papini, M.; Nookaew, I.; Siewers, V.; Nielsen, J.
Physiological characterization of recombinant Saccharomyces cerevisiae expressing the Aspergillus nidulans phosphoketolase pathway: validation of activity through 13C-based metabolic flux analysis
Appl. Microbiol. Biotechnol.
95
1001-1010
2012
Aspergillus nidulans
brenda
Kocharin, K.; Siewers, V.; Nielsen, J.
Improved polyhydroxybutyrate production by Saccharomyces cerevisiae through the use of the phosphoketolase pathway
Biotechnol. Bioeng.
110
2216-2224
2013
Aspergillus nidulans
brenda
Liu, L.; Zhang, L.; Tang, W.; Gu, Y.; Hua, Q.; Yang, S.; Jiang, W.; Yang, C.
Phosphoketolase pathway for xylose catabolism in Clostridium acetobutylicum revealed by 13C metabolic flux analysis
J. Bacteriol.
194
5413-5422
2012
Clostridium acetobutylicum (Q97JE3), Clostridium acetobutylicum, Clostridium acetobutylicum DSM 792 (Q97JE3)
brenda
Servinsky, M.D.; Germane, K.L.; Liu, S.; Kiel, J.T.; Clark, A.M.; Shankar, J.; Sund, C.J.
Arabinose is metabolized via a phosphoketolase pathway in Clostridium acetobutylicum ATCC 824
J. Ind. Microbiol. Biotechnol.
39
1859-1867
2012
Clostridium acetobutylicum (Q97JE3), Clostridium acetobutylicum, Clostridium acetobutylicum DSM 792 (Q97JE3)
brenda
Bergman, A.; Siewers, V.; Nielsen, J.; Chen, Y.
Functional expression and evaluation of heterologous phosphoketolases in Saccharomyces cerevisiae
AMB Express
6
115
2016
Bifidobacterium adolescentis (A0A0G9MEQ1), Bifidobacterium breve (A0A0L0LT01), Bifidobacterium animalis subsp. lactis (AJD88698.1), Clostridium acetobutylicum (KHD36088.1), Lactiplantibacillus plantarum (KRU18827.1), Lactiplantibacillus plantarum (KRU19755.1), Leuconostoc mesenteroides (Q5RLY5)
brenda
Rozova, O.N.; Khmelenina, V.N.; Gavletdinova, J.Z.; Mustakhimov, I.I.; Trotsenko, Y.A.
Acetate kinase-an enzyme of the postulated phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z
Antonie van Leeuwenhoek
108
965-974
2015
Methylotuvimicrobium alcaliphilum (G4T4R3), Methylotuvimicrobium alcaliphilum, Methylotuvimicrobium alcaliphilum 20Z (G4T4R3), Methylotuvimicrobium alcaliphilum 20Z
brenda
Petrareanu, G.; Balasu, M.; Vacaru, A.; Munteanu, C.; Ionescu, A.; Matei, I.; Szedlacsek, S.
Phosphoketolases from Lactococcus lactis, Leuconostoc mesenteroides and Pseudomonas aeruginosa Dissimilar sequences, similar substrates but distinct enzymatic characteristics
Appl. Microbiol. Biotechnol.
98
7855-7867
2014
Leuconostoc mesenteroides subsp. mesenteroides, Lactococcus lactis subsp. lactis (Q9CFH4), Pseudomonas aeruginosa (Q9HY13), Lactococcus lactis subsp. lactis IL1403 (Q9CFH4), Leuconostoc mesenteroides subsp. mesenteroides J18
brenda
Sarkar, P.; Roy, A.
Molecular cloning, characterization and expression of a gene encoding phosphoketolase from Termitomyces clypeatus
Biochem. Biophys. Res. Commun.
447
621-625
2014
Termitomyces clypeatus (A0A023VSP0), Termitomyces clypeatus
brenda
Henard, C.A.; Freed, E.F.; Guarnieri, M.T.
Phosphoketolase pathway engineering for carbon-efficient biocatalysis
Curr. Opin. Biotechnol.
36
183-188
2015
Bifidobacterium animalis subsp. lactis (Q9AEM9), Bifidobacterium animalis subsp. lactis DSM 101403 (Q9AEM9)
brenda
Burge, G.; Saulou-Berion, C.; Moussa, M.; Allais, F.; Athes, V.; Spinnler, H.E.
Relationships between the use of Embden Meyerhof pathway (EMP) or Phosphoketolase pathway (PKP) and lactate production capabilities of diverse Lactobacillus reuteri strains
J. Microbiol.
53
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
Metab. Eng.
41
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
Microbiology
161
430-440
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
Nat. Plants
2
15187
2015
Synechocystis sp. PCC 6803 (P74690)
brenda
Gupta, R.S.; Nanda, A.; Khadka, B.
Novel molecular, structural and evolutionary characteristics of the phosphoketolases from bifidobacteria and Coriobacteriales
PLoS ONE
12
e0172176
2017
Bifidobacterium longum (Q6R2Q7)
brenda
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.
Growth-coupled evolution of phosphoketolase to improve L-glutamate production by Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
103
8413-8425
2019
Bifidobacterium adolescentis
brenda
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