Information on EC 4.1.2.9 - phosphoketolase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.1.2.9
-
RECOMMENDED NAME
GeneOntology No.
phosphoketolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
-
Carbon fixation in photosynthetic organisms
-
-
heterolactic fermentation
-
-
Metabolic pathways
-
-
Pentose phosphate pathway
-
-
SYSTEMATIC NAME
IUBMB Comments
D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (adding phosphate; acetyl-phosphate-forming)
A thiamine-diphosphate protein.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D-Xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase
-
-
-
-
D-Xylulose-5-phosphate phosphoketolase
-
-
-
-
Pentulose-5-phosphate phosphoketolase
-
-
-
-
Pu5PPK
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9031-75-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain A187
-
-
Manually annotated by BRENDA team
Aspergillus nidulans A187
strain A187
-
-
Manually annotated by BRENDA team
strain JCM1190
EMBL
Manually annotated by BRENDA team
Bifidobacterium animalis JCM1190
strain JCM1190
EMBL
Manually annotated by BRENDA team
ATCC 19171 and CE51
-
-
Manually annotated by BRENDA team
strain NCYC 926
-
-
Manually annotated by BRENDA team
Candida parapsilosis NCYC 926
strain NCYC 926
-
-
Manually annotated by BRENDA team
Candida sp.
strain 107
-
-
Manually annotated by BRENDA team
strain 107
-
-
Manually annotated by BRENDA team
bi-functional xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
UniProt
Manually annotated by BRENDA team
Clostridium acetobutylicum DSM 792
-
UniProt
Manually annotated by BRENDA team
Clostridium acetobutylicum DSM 792
bi-functional xylulose-5-phosphate/fructose-6-phosphate phosphoketolase
UniProt
Manually annotated by BRENDA team
strain CBS 321, strain NCYC 359
-
-
Manually annotated by BRENDA team
strain S85, strain 095, strain HM2
-
-
Manually annotated by BRENDA team
Kluyveromyces phaseolosporus
strain 108
-
-
Manually annotated by BRENDA team
Kluyveromyces phaseolosporus 108
strain 108
-
-
Manually annotated by BRENDA team
Lactobacillus pentosus MD364
MD364
SwissProt
Manually annotated by BRENDA team
strain NCIMB 8826
-
-
Manually annotated by BRENDA team
strain NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum NCIMB 8826
strain NCIMB 8826
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
strain NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
-
-
Manually annotated by BRENDA team
strain ATCC 55730
-
-
Manually annotated by BRENDA team
; subsp. lactis
-
-
Manually annotated by BRENDA team
Lactococcus lactis IL 1403
; subsp. lactis
-
-
Manually annotated by BRENDA team
strain 1809
-
-
Manually annotated by BRENDA team
Lipomyces starkeyi 1809
strain 1809
-
-
Manually annotated by BRENDA team
no activity in Thiobacillus intermedius
-
-
-
Manually annotated by BRENDA team
no activity in Thiobacillus thioparus
-
-
-
Manually annotated by BRENDA team
strain GM
-
-
Manually annotated by BRENDA team
Oenococcus oeni GM
strain GM
-
-
Manually annotated by BRENDA team
CBS 4732; strain NCYC 495
-
-
Manually annotated by BRENDA team
Ogataea angusta CBS 4732
CBS 4732
-
-
Manually annotated by BRENDA team
mutants of Y-2460
-
-
Manually annotated by BRENDA team
strain 614
-
-
Manually annotated by BRENDA team
Pachysolen tannophilus 614
strain 614
-
-
Manually annotated by BRENDA team
strain WIS 54-1255
-
-
Manually annotated by BRENDA team
Penicillium chrysogenum WIS 54-1255
strain WIS 54-1255
-
-
Manually annotated by BRENDA team
strain TMB3001
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae TMB3001
strain TMB3001
-
-
Manually annotated by BRENDA team
strain A2
-
-
Manually annotated by BRENDA team
Thiobacillus sp. A2
strain A2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
C1K2N2
phylogenetic analysis of bacterial and fungal phosphoketolases, fungal phosphoketolases are of bacterial origin
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
Q97JE3
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
Clostridium acetobutylicum DSM 792
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
A0PAD9
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Q97JE3
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
the enzyme has higher activity with D-xylulose 5-phosphate than D-fructose 6-phosphate, 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
show the reaction diagram
Bifidobacterium animalis JCM1190
A0PAD9
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Clostridium acetobutylicum DSM 792
Q97JE3
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Lactococcus lactis IL 1403
-
the enzyme has higher activity with D-xylulose 5-phosphate than D-fructose 6-phosphate, the specificity constant for D-xylulose 5-phosphate is significantly higher than that for D-fructose 6-phosphate
-
-
?
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
-
-
?
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
Q9AEM9
-
-
?
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
Q88S87, Q88U67
-
-
-
?
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
C1K2N2
-
-
-
?
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
no reaction
-
-
-
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
Starkeya novella, Thiobacillus sp., Thiobacillus sp. A2
-
no reaction
-
-
-
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
Oenococcus oeni GM
-
-
-
-
-
D-ribulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Saccharomyces cerevisiae, Aspergillus nidulans, Penicillium chrysogenum, Aspergillus nidulans A187, Saccharomyces cerevisiae TMB3001, Penicillium chrysogenum WIS 54-1255
-
-
-
-
?
D-xylulose 5-phosphate
pyruvate + acetyl phosphate
show the reaction diagram
Q5B3G7
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Priceomyces medius, Kluyveromyces phaseolosporus, Cyberlindnera saturnus
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
A0PAD9
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Q88S87, Q88U67
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Q5B3G7
-
-
-
ir
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Q97JE3
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
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
show the reaction diagram
Ogataea angusta CBS 4732
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Thiobacillus sp. A2
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Lipomyces starkeyi 1809, Candida parapsilosis NCYC 926
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Bifidobacterium animalis JCM1190
A0PAD9
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Clostridium acetobutylicum DSM 792
Q97JE3
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Aspergillus nidulans A187
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Kluyveromyces phaseolosporus 108
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Oenococcus oeni GM
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Lactococcus lactis IL 1403
-
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
show the reaction diagram
Pachysolen tannophilus 614
-
-
-
-
-
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Saccharomyces cerevisiae TMB3001, Penicillium chrysogenum WIS 54-1255
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q937F6
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q9AEM9
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Lactococcus lactis, Lactococcus lactis IL 1403
-
most specific substrate
-
-
?
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
no activity
-
-
-
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
about 50% of the activity with D-xylulose 5-phosphate
-
-
-
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
higher activity than with D-xylulose 5-phosphate
-
-
-
Ribulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
approximately the same activity as with D-xylulose 5-phosphate
-
-
-
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Lactobacillus pentosus MD364
Q937F6
-
-
?
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
-
-
-
additional information
?
-
-
enzyme of the phosphoketolase pathway
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
Q88S87, Q88U67
-
-
-
?
D-xylulose 5-phosphate
pyruvate + acetyl phosphate
show the reaction diagram
Q5B3G7
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Q88S87, Q88U67
-
-
-
?
D-Xylulose 5-phosphate + phosphate
Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
Q5B3G7
-
-
-
ir
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
-
-
-
additional information
?
-
-
enzyme of the phosphoketolase pathway
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
-
required
thiamine diphosphate
-
Km: 0.000404 mM; required
thiamine diphosphate
Q88S87, Q88U67
;
thiamine diphosphate
Q5B3G7
-
thiamine diphosphate
-
; dependent on
thiamine diphosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Q88S87, Q88U67
;
Mg2+
-
stimulates
Mg2+
-
required, Km: 0.000395 mM
Mg2+
Q88S87, Q88U67
;
Mg2+
-
cofactor-bound Mg2+ is required for enzymatic activity
Mn2+
Q88S87, Q88U67
;
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
-
no inhibition
acetyl-CoA
-
-
Dodecanoyl-CoA
-
-
erythrose 4-phosphate
-
-
fructose 6-phosphate
-
competitive to xylulose 5-phosphate
glyceraldehyde 3-phosphate
-
-
Mn2+
-
strong inhibition above 1 mM
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
phosphoenolpyruvate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calcium thiamine diphosphate
Q88S87, Q88U67
;
-
EDTA
-
stimulates
magnesium thiamine diphosphate
Q88S87, Q88U67
;
-
manganese thiamine diphosphate
Q88S87, Q88U67
;
-
phosphate
-
required
phosphate
-
Km: 5.55 mM; required
Sodium borate
-
stimulate
sulfhydryl compounds
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
D-fructofuranose 6-phosphate
Q88S87, Q88U67
apparent Km value, Mg2+
0.0004
D-fructose 6-phosphate
Q88S87, Q88U67
apparent Km value, Mn2+
0.16
D-fructose 6-phosphate
Q88S87, Q88U67
apparent Km value, Ca2+
10
D-fructose 6-phosphate
Q9AEM9
37C, pH 6.5
24
D-fructose 6-phosphate
Q88S87, Q88U67
D-fructose 6-phosphate and phosphate
1.25
D-xylulose 5-phosphate
-
-
1.6
D-xylulose 5-phosphate
-
-
2.4
D-xylulose 5-phosphate
-
-
3.6
D-xylulose 5-phosphate
Q88S87, Q88U67
xylulose 5-phosphate and phosphate
4.27
D-xylulose 5-phosphate
-
-
4.7
D-xylulose 5-phosphate
-
-
45
D-xylulose 5-phosphate
Q9AEM9
37C, pH 6.5
22
fructose 6-phosphate
-
-
29
fructose 6-phosphate
-
-
2.9
phosphate
Q88S87, Q88U67
D-fructose 6-phosphate and phosphate
7.5
phosphate
Q88S87, Q88U67
xylulose 5-phosphate and phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.052
Q88S87, Q88U67
purification step crude extract, histidine tail phosphoketolase-2
0.144
-
activity with fructose 6-phosphate
0.152
-
activity with ribulose 5-phosphate
0.2
Q88S87, Q88U67
purification step Biogel P6 column, histidine tail phosphoketolase-2
0.591
-
activity with xylulose 5-phosphate
0.61
Q88S87, Q88U67
purification step Sephacryl-300 column, histidine tail phosphoketolase-2
2.01
Q97JE3
pH 6.5, 37C
2.3
-
activity with xylulose 5-phosphate
6.9
Q97JE3
substrate D-xylulose 5-phosphate, pH 6.5, 37C
21
Q97JE3
substrate D-fructose 6-phosphate, pH 6.5, 37C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7
-
pH 5.5: about 50% of maximal activity, pH 7.0: about 45% of maximal activity
5.5 - 7
-
about 40% of maximal activity at pH 5.5 and at pH 7.0
6 - 7
-
pH 6.0: maximal activity, little activity above pH 7.0
6.4 - 8.2
-
about 50% of maximal activity at pH 6.4 and 8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Q88S87, Q88U67
enzyme assay; enzyme assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27.5 - 32.5
-
27.5C: about 70% of maximal activity, 32.5C: about 30% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
gel filtration
37324
55000
-
calculation from ultracentrifugation data
37328
88700
Q937F6
calculated from amino acid sequence
649379
90000
Q937F6
SDS-PAGE
649379
90000
Q88S87, Q88U67
SDS-PAGE
691198
92450
C1K2N2
calculated
703478
550000
Q9AEM9
gel filtration
651682
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 95727, calculated from amino acid sequence
?
Lactococcus lactis IL 1403
-
x * 95727, calculated from amino acid sequence
-
hexamer
Q9AEM9
6 * 90000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 17% (w/v) PEG 3350 and 0.2 M NaSCN, at 18C
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5.5
-
most stable in the range
37327
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
phosphate is essential for stability
-
5097
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-55C, several years with little loss of activity
-
thioglycerol, 12 mM, required for long-term storage
-
4C, 24 h, 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Q88S87, Q88U67
HisTrap HP column chromatography and Superdex 200 gel filtration; HisTrap Ni2+ metal affinity column chromatography and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Corynebacterium glutamicum
A0PAD9
expression in Escherichia coli
Q937F6
into the vector pET21a+ for expression in Escherichia coli BL21DE3 cells; into the vectors pET21a+ and pET28b+ for expression in Escherichia coli BL21DE3 cells
Q88S87, Q88U67
expressed in Escherichia coli BL21 (DE3) RIL cells; expressed in Escherichia coli BL21(DE3) RIL cells
-
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
-
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
Q97JE3
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
Clostridium acetobutylicum DSM 792
-
-
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
C1K2N2
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
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
-
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
-
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
Lactobacillus plantarum NCIMB 8826
-
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, 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
Lactobacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
polyketide natural products play an important role in the treatment of a wide range of human physiological disorders
synthesis
-
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
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
Lactobacillus 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, 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
Lactobacillus plantarum NCIMB 8826 delta ldhL1 -xpk1::tkt-delta xpk
-
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
-
synthesis
-
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