Information on EC 4.1.2.22 - fructose-6-phosphate phosphoketolase

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

EC NUMBER
COMMENTARY hide
4.1.2.22
-
RECOMMENDED NAME
GeneOntology No.
fructose-6-phosphate phosphoketolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Fructose 6-phosphate + phosphate = acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
of an aldehyde, C-C bond cleavage
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bifidobacterium shunt
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Carbon fixation in photosynthetic organisms
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
D-fructose-6-phosphate D-erythrose-4-phosphate-lyase (adding phosphate; acetyl-phosphate-forming)
Also acts on D-xylulose 5-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-57-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain MTCC 5423
-
-
Manually annotated by BRENDA team
strain BluCI/TPT (DSM 19703T, ATCC BAA-1567T)
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-
Manually annotated by BRENDA team
strain BluCI/TPT (DSM 19703T, ATCC BAA-1567T)
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
BB536
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strains YIT 10443T (JCM 15461T, DSM 21395T) and YIT 10738
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-
Manually annotated by BRENDA team
Candida sp.
strain 107
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-
Manually annotated by BRENDA team
strain 107
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain C7
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-
Manually annotated by BRENDA team
strain C7
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain C7
SwissProt
Manually annotated by BRENDA team
strain C7
SwissProt
Manually annotated by BRENDA team
no activity in Actinomyces turicensis-like bacteria
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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fructose 6-phosphate phosphoketolase activity is present in 24 porcine wild-type strains of Lactobacillus reuteri and Lactobacillus mucosae, but not in the Lactobacillus salivarius or in L. reuteri ATCC strains. The activity of fructose 6-phosphate phosphoketolase increases after treatment of the culture at low pH and diminishes after porcine bile-salts stress conditions in wild-type strains of Lactobacillus reuteri
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
key enzyme of the bifid-shunt
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-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
D-fructose 6-phosphate + phosphate
acetyl phosphate + H2O + erythrose 4-phosphate
show the reaction diagram
D-ribose 5-phosphate + phosphate
?
show the reaction diagram
D-xylulose 5-phosphate + 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 + H2O + D-glyceraldehyde 3-phosphate
show the reaction diagram
Fructose 1-6-diphosphate + phosphate
?
show the reaction diagram
Sedoheptulose 7-phosphate + phosphate
?
show the reaction diagram
Xylulose 5-phosphate + phosphate
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
key enzyme of the bifid-shunt
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D6PAH1
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-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
contains Ca2+ bound to the active site
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
ATP
-
phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site
hydroxylamine
Iodosobenzoate
oxaloacetic acid
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phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site. AMP and phosphoenolpyruvate/oxaloacetic acid operate independently, with AMP activating Xfp2 and phosphoenolpyruvate/oxaloacetic acid inhibiting the activated enzyme
p-hydroxymercuribenzoate
phosphoenolpyruvate
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phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site. AMP and phosphoenolpyruvate/oxaloacetic acid operate independently, with AMP activating Xfp2 and phosphoenolpyruvate/oxaloacetic acid inhibiting the activated enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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acts as a very potent activator, 20 microM AMP is capable of increasing Xfp2 activity by 24.8%, while 50 microM prevent inhibition caused by 0.6 mM ATP. AMP and phosphoenolpyruvate/oxaloacetic acid operate independently, with AMP activating Xfp2 and phosphoenolpyruvate/oxaloacetic acid inhibiting the activated enzyme
thiamin diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4 - 53.5
D-fructose 6-phosphate
45
D-xylulose 5-phosphate
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pH 6.5, 37C
1.4 - 39
fructose 6-phosphate
0.52 - 25.5
phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 25.7
D-fructose 6-phosphate
25.7
phosphate
Bifidobacterium breve
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in 40 mM potassium phosphate pH 6.5, 25 mM MES buffer pH 6.5, 0.02 mM ThDP and 0.1 mM MgCl2, at 22C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
ATP
Cryptococcus neoformans
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pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.28
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D-fructose 6-phosphate as substrate
6.2
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crude cell extract, at 37C
147.3
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after 23.7fold purification, at 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
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using D-fructose 6-phosphate as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
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about 30% of maximal activity at pH 4.0 and at pH 9.0
4 - 8
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pH 4.0: about 40% of maximal activity, pH 9.0: about 30% of maximal activity
4.5 - 7
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pH 4.5: about 45% of maximal activity, pH 7.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme is partially associated with cytoplasmic membrane through weak interactions, activity is higher in bile resistant strains
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
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gel filtration
200000
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three active peaks appear on gel filtration chromatography with estimated native molecular masses of 200 kDa (homodimer), 350 kDa (homotetramer) and 600 kDa (homohexamer)
300000
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gel filtration
350000
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three active peaks appear on gel filtration chromatography with estimated native molecular masses of 200 kDa (homodimer), 350 kDa (homotetramer) and 600 kDa (homohexamer)
600000
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three active peaks appear on gel filtration chromatography with estimated native molecular masses of 200 kDa (homodimer), 350 kDa (homotetramer) and 600 kDa (homohexamer)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 90000, SDS-PAGE
hexamer
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6 * 90000, SDS-PAGE
homodimer
homohexamer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cryocrystallography technique, using 24% (w/v) PEG 6000, 0.1 M bicine buffer, pH 9.0
sitting drop vapor diffusion method, using 0.05 mM thiamine diphosphate, 0.25 mM MgCl2, 24% (w/v) PEG 6000 and 0.1 M Bicine pH 9.0, at 20C
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using 10 mg/ml thiamine diphosphate, 4% (v/v) Tacsimate pH 5.0, 12% (w/v) polyethylene glycol 3350 for the native enzyme. Se-Met substituted protein crystals are grown with 17% (w/v) polyethylene glycol 3350, 0.1 M MES (pH6.6), 0.2 M sodium thiocyanate in the absence of thiamine diphosphate
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GSTrap HP affinity column chromatography
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HisTrap column chromatography, MonoQ column chromatography, and Superdex 200 gel filtration
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Ni-NTA column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21 CodonPlus (DE3)-RIL cells
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expressed in Escherichia coli strain BL21 (DE3)
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expression in Escherichia coli
selenomethionine-labeled enzyme is expressed in Escherichia coli B834 (DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H142A
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
H142N
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
H548A
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
Q321A
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
S440A
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
Y501F
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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the gene encoding xylulose-5-phosphate/fructose-6-phosphate phosphoketolase (xfp) is conserved among Bifidobacterium species within a more variable region of the genome, useful for strain identification
Show AA Sequence (124 entries)
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