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
4.1.2.22
-
RECOMMENDED NAME
GeneOntology No.
fructose-6-phosphate phosphoketolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Fructose 6-phosphate + phosphate = acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
-
Carbon fixation in photosynthetic organisms
-
-
Microbial metabolism in diverse environments
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F6PPK
-
-
-
-
Fructose-6-phosphate phosphoketolase
-
-
-
-
Phosphoketolase, fructose 6-phosphate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37290-57-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain MTCC 5423
-
-
Manually annotated by BRENDA team
Bifidobacterium adolescentis MTCC 5423
strain MTCC 5423
-
-
Manually annotated by BRENDA team
strain BluCI/TPT (DSM 19703T, ATCC BAA-1567T)
-
-
Manually annotated by BRENDA team
Bifidobacterium bombi BluCI/TPT
strain BluCI/TPT (DSM 19703T, ATCC BAA-1567T)
-
-
Manually annotated by BRENDA team
Bifidobacterium breve 203
-
-
-
Manually annotated by BRENDA team
strain DSM 20219
-
-
Manually annotated by BRENDA team
Bifidobacterium longum BB536
BB536
-
-
Manually annotated by BRENDA team
Bifidobacterium longum JCM1217
-
-
-
Manually annotated by BRENDA team
strains YIT 10443T (JCM 15461T, DSM 21395T) and YIT 10738
-
-
Manually annotated by BRENDA team
CECT4549 and bile resistant strains
-
-
Manually annotated by BRENDA team
Candida sp.
strain 107
-
-
Manually annotated by BRENDA team
strain 107
-
-
Manually annotated by BRENDA team
Lactobacillus paraplantarum C7
strain C7
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides C7
strain C7
SwissProt
Manually annotated by BRENDA team
no activity in Actinomyces turicensis-like bacteria
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
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)
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
-
-
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Q9AEM9
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
D6PAH1
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Bifidobacterium longum BB536
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Lactobacillus paraplantarum C7
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Bifidobacterium adolescentis MTCC 5423
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Bifidobacterium longum JCM1217
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + phosphate
?
show the reaction diagram
-
key enzyme of the bifid-shunt
-
-
-
D-fructose 6-phosphate + phosphate
acetyl phosphate + H2O + erythrose 4-phosphate
show the reaction diagram
Bifidobacterium breve, Bifidobacterium breve 203
-
-
-
-
?
D-ribose 5-phosphate + phosphate
?
show the reaction diagram
-
13.3% of the activity with D-fructose 6-phosphate
-
-
-
D-ribose 5-phosphate + phosphate
?
show the reaction diagram
-
25% of the activity with D-fructose 6-phosphate, 208% of the activity with D-fructose 6-phosphate
-
-
-
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 + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D6PAH1
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Bifidobacterium longum JCM1217
-
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + H2O + D-glyceraldehyde 3-phosphate
show the reaction diagram
Bifidobacterium breve, Bifidobacterium breve 203
-
-
-
-
?
Fructose 1-6-diphosphate + phosphate
?
show the reaction diagram
-
13.3% of the activity with D-fructose 6-phosphate
-
-
-
Sedoheptulose 7-phosphate + phosphate
?
show the reaction diagram
-
13.3% of the activity with D-fructose 6-phosphate
-
-
-
Sedoheptulose 7-phosphate + phosphate
?
show the reaction diagram
-
16.6% of the activity with D-fructose 6-phosphate
-
-
-
Xylulose 5-phosphate + phosphate
?
show the reaction diagram
-
166% of the activity with D-fructose 6-phosphate
-
-
-
Xylulose 5-phosphate + phosphate
?
show the reaction diagram
-
6.6% of the activity with D-fructose 6-phosphate
-
-
-
Fructose 1-6-diphosphate + phosphate
?
show the reaction diagram
-
20.8% of the activity with D-fructose 6-phosphate
-
-
-
additional information
?
-
-
key enzyme of carbohydrate catabolism
-
-
-
additional information
?
-
Q5RLY5
key enzyme of carbohydrate catabolism
-
-
-
additional information
?
-
-
existence of both substrate cooperativity for all three substrates and allosteric regulation through the binding of effector molecules at sites separate from the active site
-
-
-
additional information
?
-
Leuconostoc mesenteroides C7
Q5RLY5
key enzyme of carbohydrate catabolism
-
-
-
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
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
Q9AEM9
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
-
-
-
-
?
D-Fructose 6-phosphate + phosphate
Acetyl phosphate + D-erythrose 4-phosphate + H2O
show the reaction diagram
D6PAH1
-
-
-
?
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
Bifidobacterium adolescentis MTCC 5423
-
-
-
-
?
D-xylulose 5-phosphate + phosphate
acetyl phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D6PAH1
-
-
-
?
additional information
?
-
-
key enzyme of carbohydrate catabolism
-
-
-
additional information
?
-
Leuconostoc mesenteroides, Leuconostoc mesenteroides C7
Q5RLY5
key enzyme of carbohydrate catabolism
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
-
required
thiamine diphosphate
-
-
thiamine diphosphate
-
dependent on
thiamine diphosphate
D6PAH1
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
contains Ca2+ bound to the active site
Mg2+
-
slight stimulation
Mg2+
-
45% of the activation with Mn2+
Mg2+
-
maximal activation in presence of Mg2+
Mg2+
-
required
Mn2+
-
maximal activation with Mn2+
Mn2+
-
44% of the activation with Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
phosphoenolpyruvate and oxaloacetic acid share the same or have overlapping allosteric binding sites, while ATP binds at a separate site
oxaloacetic acid
-
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
phosphoenolpyruvate
-
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
LITERATURE
IMAGE
AMP
-
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
-
slight stimulation
thiamin diphosphate
-
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
D-fructose 6-phosphate
D6PAH1
mutant enzyme Y501F, pH and temperature not specified in the publication
2.3
D-fructose 6-phosphate
D6PAH1
mutant enzyme H548A, pH and temperature not specified in the publication
4.4
D-fructose 6-phosphate
D6PAH1
mutant enzyme Q321A, pH and temperature not specified in the publication
5.08
D-fructose 6-phosphate
-
in 71 mM sodium fluoride and 24 mM sodium iodoacetate, at 37C
7.2
D-fructose 6-phosphate
D6PAH1
mutant enzyme H142N, pH and temperature not specified in the publication
7.4
D-fructose 6-phosphate
D6PAH1
mutant enzyme H142A, pH and temperature not specified in the publication
9.7
D-fructose 6-phosphate
-
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
9.7
D-fructose 6-phosphate
D6PAH1
wild type enzyme, pH and temperature not specified in the publication
10
D-fructose 6-phosphate
-
pH 6.5, 37C
53.5
D-fructose 6-phosphate
D6PAH1
mutant enzyme S440A, pH and temperature not specified in the publication
45
D-xylulose 5-phosphate
-
pH 6.5, 37C
1.4
fructose 6-phosphate
-
-
2.5
fructose 6-phosphate
-
-
39
fructose 6-phosphate
-
-
0.52
phosphate
D6PAH1
mutant enzyme H548A, pH and temperature not specified in the publication
0.57
phosphate
D6PAH1
mutant enzyme S440A, pH and temperature not specified in the publication
0.87
phosphate
-
-
1.2
phosphate
-
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
1.2
phosphate
D6PAH1
wild type enzyme, pH and temperature not specified in the publication
1.6
phosphate
D6PAH1
mutant enzyme Q321A, pH and temperature not specified in the publication
1.7
phosphate
D6PAH1
mutant enzyme H142A, pH and temperature not specified in the publication
2.6
phosphate
D6PAH1
mutant enzyme H142N, pH and temperature not specified in the publication
25.5
phosphate
D6PAH1
mutant enzyme Y501F, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
D-fructose 6-phosphate
D6PAH1
mutant enzyme H142A, pH and temperature not specified in the publication
0.65
D-fructose 6-phosphate
D6PAH1
mutant enzyme H142N, pH and temperature not specified in the publication
0.99
D-fructose 6-phosphate
D6PAH1
mutant enzyme Q321A, pH and temperature not specified in the publication
1.67
D-fructose 6-phosphate
D6PAH1
mutant enzyme H548A, pH and temperature not specified in the publication
3.28
D-fructose 6-phosphate
D6PAH1
mutant enzyme Y501F, pH and temperature not specified in the publication
5.83
D-fructose 6-phosphate
D6PAH1
mutant enzyme S440A, pH and temperature not specified in the publication
25.67
D-fructose 6-phosphate
D6PAH1
wild type enzyme, pH and temperature not specified in the publication
25.7
D-fructose 6-phosphate
-
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
25.7
phosphate
-
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
LITERATURE
IMAGE
0.6
ATP
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.28
-
D-fructose 6-phosphate as substrate
6.2
-
crude cell extract, at 37C
147.3
-
after 23.7fold purification, at 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.5
-
using D-fructose 6-phosphate as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
pH 4.0: about 40% of maximal activity, pH 9.0: about 30% of maximal activity
4 - 9
-
about 30% of maximal activity at pH 4.0 and at pH 9.0
4.5 - 7
-
pH 4.5: about 45% of maximal activity, pH 7.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is partially associated with cytoplasmic membrane through weak interactions, activity is higher in bile resistant strains
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
88700
-
SDS-PAGE
681361
90000
-
-
664983
160000
-
gel filtration
5096
200000
-
three active peaks appear on gel filtration chromatography with estimated native molecular masses of 200 kDa (homodimer), 350 kDa (homotetramer) and 600 kDa (homohexamer)
713652
290000
-
gel filtration
5096
300000
-
gel filtration
653088
350000
-
three active peaks appear on gel filtration chromatography with estimated native molecular masses of 200 kDa (homodimer), 350 kDa (homotetramer) and 600 kDa (homohexamer)
713652
550000
-
gel filtration
651682
600000
-
three active peaks appear on gel filtration chromatography with estimated native molecular masses of 200 kDa (homodimer), 350 kDa (homotetramer) and 600 kDa (homohexamer)
713652
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 90000, SDS-PAGE
hexamer
-
6 * 90000, SDS-PAGE
homodimer
-
2 * 92500, SDS-PAGE
homodimer
D6PAH1
x-ray crystallography
homodimer
Bifidobacterium longum JCM1217
-
2 * 92500, SDS-PAGE
-
homohexamer
-
6 * 90000, SDS-PAGE, 6 * 92700, calculated from amino acid sequence
homohexamer
Bifidobacterium breve 203
-
6 * 90000, SDS-PAGE, 6 * 92700, calculated from amino acid sequence
-
tetramer
-
alpha2,beta2, 2 * 93000 + 2 * 59000, SDS-PAGE
tetramer
Bifidobacterium longum BB536
-
alpha2,beta2, 2 * 93000 + 2 * 59000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cryocrystallography technique, using 24% (w/v) PEG 6000, 0.1 M bicine buffer, pH 9.0
D6PAH1
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
-
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57
-
5 min, 40% loss of activity
5096
65
-
5 min, about 45% loss of activity
5096
65
-
5 min, about 65% loss of activity
5096
80
-
5 min, complete loss of activity
5096
80
-
5 min, about 85% loss of activity
5096
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
-
HisTrap column chromatography, MonoQ column chromatography, and Superdex 200 gel filtration
-
GSTrap HP affinity column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 CodonPlus (DE3)-RIL cells
-
selenomethionine-labeled enzyme is expressed in Escherichia coli B834 (DE3) cells
D6PAH1
expressed in Escherichia coli
-
expressed in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli
Q5RLY5
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E479A
D6PAH1
inactive
H142A
D6PAH1
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
H142N
D6PAH1
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
H320A
D6PAH1
inactive
H320N
D6PAH1
inactive
H548A
D6PAH1
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
H553A
D6PAH1
inactive
H553N
D6PAH1
inactive
H64A
D6PAH1
inactive
H64N
D6PAH1
inactive
H97A
D6PAH1
inactive
H97N
D6PAH1
inactive
K605A
D6PAH1
inactive
N549A
D6PAH1
inactive
Q321A
D6PAH1
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
S440A
D6PAH1
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
Y501F
D6PAH1
the mutant shows reduced kcat with D-fructose 6-phosphate compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
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