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Information on EC 2.7.1.105 - 6-phosphofructo-2-kinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9MB58

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EC Tree
IUBMB Comments
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9MB58
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
6-phosphofructo-2-kinase, phosphofructokinase 2, phosphofructokinase-2, upfk-2, inducible 6-phosphofructo-2-kinase, fructose 6-phosphate 2-kinase, ipfk2, tpfk-2, phosphofructokinase-2/fructose bisphosphatase-2, 6-phosphofructose 2-kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
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-
-
-
6-phosphofructose 2-kinase
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-
-
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ATP:D-fructose-6-phosphate 2-phosphotransferase
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-
-
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fructose 6-phosphate 2-kinase
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-
-
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kinase, 6-phosphofructo-2-(phosphorylating)
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-
-
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phosphofructokinase 2
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
ATP:beta-D-fructose-6-phosphate 2-phosphotransferase
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
78689-77-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
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-
?, r
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dihydroxyacetone phosphate
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diphosphate
not phosphate
glycerate 2-phosphate
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phosphoenolpyruvate
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sn-glycerol 3-phosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
ATP
pH 6.0, 25°C
0.5
beta-D-fructose 6-phosphate
pH 6.0, 25°C
additional information
additional information
comparison of Km of wild-type and mutant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.35
dihydroxyacetone phosphate
pH 6.0, 25°C
0.45
glycerate 2-phosphate
pH 6.0, 25°C
0.13
phosphoenolpyruvate
pH 6.0, 25°C
0.35
sn-glycerol 3-phosphate
pH 6.0, 25°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F26_ARATH
744
0
82559
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
370000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 83000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the deletion of N-terminal 318 amino acids abolishes the Michaelis-Menten kinetics of enzyme, Km of beta-D-fructose 6-phosphate is increased, whereas Km of ATP is not significantly altered. When the first 66 amino acids are deleted, the activity ration between 6-phosphofructo-2-kinase and beta-D-fructose 2,6-bisphosphatase is halved. The deletion of 125, 179, 249 and 318 amino acids results in progressive further decreases in the activity ratio and the activity ratio is reduced 4fold when N-terminus is deleted completely. The full-length enzyme is eluted as a tetramer, whereas the truncated enzymes are eluted as monomers
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
about 76% of enzyme activity remains after 10 min, both in the absence and in the presence of phosphate
4
10 min, enzyme is stable, both in the absence and in the presence of phosphate
42
10 min, activation of enzyme and deletion mutant decreases rapidly, but the presence of phosphate protectes the enzyme activities from inactivation and 75% of enzyme activity remains after 15 min
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Villadsen, D.; Nielsen, T.H.
N-terminal truncation affects the kinetics and structure of fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana
Biochem. J.
359
591-597
2001
Arabidopsis thaliana (Q9MB58)
Manually annotated by BRENDA team