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Information on EC 2.7.1.90 - diphosphate-fructose-6-phosphate 1-phosphotransferase and Organism(s) Entamoeba histolytica and UniProt Accession Q27651
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2.7.1.90 diphosphate-fructose-6-phosphate 1-phosphotransferaseIUBMB Comments
The enzyme catalyses a similar reaction to EC 2.7.1.11, 6-phosphofructokinase, but utilizes diphosphate instead of ATP as the the phosphate donor. It has been described in higher plants, primitive eukaryotes, bacteria, and archaea.
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Word Map
- 2.7.1.90
- 2,6-bisphosphate
- atp-pfks
- propionibacterium
- freudenreichii
- fructose-2,6-bisphosphate
-
phosphofructokinases
- dikinase
-
embden-meyerhof-parnas
- fowleri
- methanolica
-
thermoproteus
-
mgppi
- tenax
The taxonomic range for the selected organisms is: Entamoeba histolytica
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ppi-pfk, pyrophosphate-dependent phosphofructokinase, ppi-dependent phosphofructokinase, pyrophosphate:fructose-6-phosphate 1-phosphotransferase, pyrophosphate:fructose 6-phosphate 1-phosphotransferase, pyrophosphate fructose-6-phosphate 1-phosphotransferase, pyrophosphate fructose 6-phosphate 1-phosphotransferase, inorganic pyrophosphate-dependent phosphofructokinase, pyrophosphate-dependent fructose-6-phosphate 1-phosphotransferase, pyrophosphate-dependent 6-phosphofructokinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-phosphofructokinase (pyrophosphate)
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-
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diphosphate-D-fructose-6-phosphate 1-phosphotransferase
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-
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inorganic pyrophosphate-dependent phosphofructokinase
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inorganic pyrophosphate-phosphofructokinase
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phosphotransferase, pyrophosphate-D-fructose 6-phosphate 1-
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pyrophosphate D-fructose-6-phosphate 1-phosphotransferase
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-
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pyrophosphate-D-fructose 6-phosphate 1-phosphotransferase
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pyrophosphate-D-fructose 6-phosphate phosphotransferase
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pyrophosphate-dependent phosphofructo-1-kinase
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pyrophosphate-dependent phosphofructokinase
pyrophosphate:D-fructose-6-phosphate 1-phosphotransferase
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-
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pyrophosphate-dependent phosphofructokinase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate
random bi bi mechanism
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diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate
Met249 plays a critical role in the binding of fructose 6-phosphate and the stabilization of the transition state
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diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate
Arg423 and Tyr 420 are involved in substrate binding and catalytic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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-, -
SYSTEMATIC NAME
IUBMB Comments
diphosphate:D-fructose-6-phosphate 1-phosphotransferase
The enzyme catalyses a similar reaction to EC 2.7.1.11, 6-phosphofructokinase, but utilizes diphosphate instead of ATP as the the phosphate donor. It has been described in higher plants, primitive eukaryotes, bacteria, and archaea.
CAS REGISTRY NUMBER
COMMENTARY
55326-40-4
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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
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
specific for diphosphate as phosphor donor
-
?
diphosphate + 2,5-anhydro-D-mannitol 6-phosphate
phosphate + 2,5-anhydro-D-mannitol 1,6-bisphosphate
-
-
-
r
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-diphosphate
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-
-
-
r
diphosphate + D-sedoheptulose 7-phosphate
phosphate + D-sedoheptulose 1,7-bisphosphate
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-
-
r
phosphate + D-fructose 1,6-diphosphate
diphosphate + D-fructose 6-phosphate
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-
-
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r
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
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-
-
?
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
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-
-
?
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
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-
-
?
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
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no phosphate group exchange reaction between phosphate and diphosphate, or D-fructose 6-phosphate and D-fructose 1,6-bisphosphate in absence of a third substrate
arsenate can replace phosphate in the reverse reaction
r
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
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specific for diphosphate as phosphor donor
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?
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
-
specific for diphosphate as phosphor donor
-
?
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
-
specific for diphosphate as phosphor donor
-
r
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
-
specific for diphosphate as phosphor donor
-
r
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
-
specific for diphosphate as phosphor donor
arsenate can replace phosphate in the reverse reaction
r
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
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
-
-
-
?
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
-
-
-
?
diphosphate + D-fructose 6-phosphate
phosphate + D-fructose 1,6-bisphosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
divalent cations
Mg2+
additional information
Mg2+
-
enzyme requires 0.5 mM in the forward reaction, 0.0008 mM in the reverse reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 6-phosphate
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competitive versus D-fructose 1,6-bisphosphate and phosphate
3-[N-(2-phenylthioethyl)-N-methylamino]-1-hydroxypropylidene-1,1-bisphosphonate
inhibition of growth
3-[N-(2-phenylthioethyl)-N-methylamino]-1-hydroxypropylidene-1,1-bisphosphonate
i.e. CGP 48048, bisphosphonate, synthetic diphosphate analogue
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km values for substrates of mutant enzymes
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0.045
D-fructose 6-phosphate
recombinant His-tagged enzyme, pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat values of mutant enzymes
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
3-[N-(2-phenylthioethyl)-N-methylamino]-1-hydroxypropylidene-1,1-bisphosphonate
pH 7.0, 25°C
0.16
D-fructose 6-phosphate
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versus D-fructose 1,6-bisphosphate, pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PFKA_ENTHI
436
0
47670
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H415A
-
site-directed mutagenesis, reduced activity, increased Km for fructose 6-phosphate and decreased Km for diphosphate
H416A
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site-directed mutagenesis, reduced activity, slightly increased Km for fructose 6-phosphate
K408A
-
site-directed mutagenesis, activity , decreased Km for diphosphate
M249A
-
site-directed mutagenesis, reduced activity and increased Km-value for fructose 6-phosphate compared to wild-type
M249I
-
site-directed mutagenesis, highly reduced activity, increased Km-value for fructose 6-phosphate compared to wild-type
M249L
-
site-directed mutagenesis, highly reduced activity and increased Km-value for fructose 6-phosphate compared to wild-type
R377A
-
site-directed mutagenesis, increased Km values for fructose 6-phosphate and diphosphate
R405A
-
site-directed mutagenesis, increased activity, kinetic properties similar to the wild-type
R423A
-
site-directed mutagenesis, decrease of kcat by 10000fold, 10fold increased Km for diphosphate, 126fold increased Km for fructose 6-phosphate
S392A
-
site-directed mutagenesis, activity and kinetic properties similar to the wild-type
Y420A
-
site-directed mutagenesis, reduced activity, increased Km values for fructose 6-phosphate and diphosphate
Y420F
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site-directed mutagenesis, reduced activity, increased Km for fructose 6-phosphate, decreased Km for diphosphate
Y420H
-
site-directed mutagenesis, reduced activity, increased Km values for fructose 6-phosphate and diphosphate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is stable if whole cells are lyophilized or vigorously sonicated
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% v/v glycerol, less than 50% loss of activity within 2 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native, partial 146fold, further purification leads to inactivation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, functional expression in Escherichia coli BL21(DE3) as His-tagged protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reeves, R.E.; South, D.J.; Blytt, H.J.; Warren, L.G.
Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase. A new enzyme with the glycolytic function of 6-phosphofructokinase
J. Biol. Chem.
249
7737-7741
1974
Entamoeba histolytica, Entamoeba histolytica H200
Reeves, R.E.; Serrano, R.; South, D.J.
6-Phosphofructokinase (pyrophosphate). Properties of the enzyme from Entamoeba histolytica and its reaction mechanism
J. Biol. Chem.
251
2958-2962
1976
Entamoeba histolytica, Entamoeba histolytica DKB
Reeves, R.E.; Lobelle-Rich, P.; Eubank, W.B.
6-Phosphofructokinase (pyrophosphate) from Entamoeba histolytica
Methods Enzymol.
90
97-102
1982
Entamoeba histolytica, Entamoeba histolytica K-9 / ATCC 30015
-
Bruchhaus, I.; Jacobs, T.; Denart, M.; Tannich, E.
Pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica: molecular cloning, recombinant expression and inhibition by pyrophosphate analogs
Biochem. J.
316
57-63
1996
Entamoeba histolytica (Q27651)
-
Wang, X.; Deng, Z.; Kemp, R.G.
An essential methionine residue involved in substrate binding by phosphofructokinases
Biochem. Biophys. Res. Commun.
250
466-468
1998
Entamoeba histolytica
Deng, Z.; Wang, X.; Kemp, R.G.
Site-directed mutagenesis of the fructose 6-phosphate binding site of the pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica
Arch. Biochem. Biophys.
380
56-62
2000
Entamoeba histolytica
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