Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chevalier, N.; Bertrand, L.; Rider, M.H.; Opperdoes, F.R.; Rigden, D.J.; Michels, P.A.
    6-Phosphofructo-2-kinase and fructose-2,6-bisphosphatase in Trypanosomatidae. Molecular characterization, database searches, modelling studies and evolutionary analysis (2005), FEBS J., 272, 3542-3560.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.105 DNA and amino acid sequence determination and analysis Trypanosoma brucei
2.7.1.105 DNA and amino acid sequence determination and analysis, phylogenetic analysis of the 6-phosphofructo-2-kinase and the fructose-2,6-bisphosphatase domains, expression of His-tagged wild-type and mutant isozymes Tb1, Tb2, and Tb4 in Escherichia coli, poor expression levels and mostly inactive and unstable isozymes, e.g. recombinant Tb2 is inactive Trypanosoma brucei
3.1.3.46 bifunctional enzyme, isozymes 1-4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged isozymes 1-4 in Escherichia coli Trypanosoma brucei
3.1.3.46 DNA and amino acid sequence determination and analysis, phylogenetic analysis Trypanosoma cruzi
3.1.3.46 DNA and amino acid sequence determination and analysis, phylogenetic analysis Leishmania major

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 citrate 60% inhibition at 1 mM Trypanosoma brucei
2.7.1.105 glycerol 3-phosphate 20% inhibition at 2mM Trypanosoma brucei
2.7.1.105 additional information enzyme is not affected by protein kinase C Trypanosoma brucei
2.7.1.105 phosphoenolpyruvate
-
 Trypanosoma brucei
2.7.1.105 protein kinase A inactivation via a 7fold increase in Km for fructose 6-phosphate without alteration of Vmax Trypanosoma brucei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.105 0.88
-
 ATP 30°C Trypanosoma brucei
2.7.1.105 1.62
-
 ATP pH 7.1, 30°C, recombinant isozyme Tb1 Trypanosoma brucei
2.7.1.105 1.9 4.6 beta-D-fructose 6-phosphate pH 7.1, 30°C, recombinant isozyme Tb1 Trypanosoma brucei
2.7.1.105 5.8
-
 beta-D-fructose 6-phosphate pH 7.1, 30°C Trypanosoma brucei
2.7.1.105 39
-
 beta-D-fructose 6-phosphate pH 7.1, 30°C, protein kinase A treated enzyme Trypanosoma brucei
3.1.3.46 additional information
-
 additional information kinetic analysis Trypanosoma brucei
3.1.3.46 additional information
-
 additional information kinetic analysis Trypanosoma cruzi
3.1.3.46 additional information
-
 additional information kinetic analysis Leishmania major

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.105 cytosol
-
 Trypanosoma brucei 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.105 Mg2+
-
 Trypanosoma brucei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.105 54000
-
 x * 72000, isozyme Tb2, about, sequence calculation, x * 54000, isozyme Tb3, about, sequence calculation, x * 79000, isozyme Tb4, about, sequence calculation Trypanosoma brucei
2.7.1.105 60000
-
 2 * 60000, recombinant Tb1, SDS-PAGE, 2 * 111000, isozyme Tb1, about, sequence calculation Trypanosoma brucei
2.7.1.105 72000
-
 x * 72000, isozyme Tb2, about, sequence calculation, x * 54000, isozyme Tb3, about, sequence calculation, x * 79000, isozyme Tb4, about, sequence calculation Trypanosoma brucei
2.7.1.105 76400
-
 gel filtration Trypanosoma brucei
2.7.1.105 79000
-
 x * 72000, isozyme Tb2, about, sequence calculation, x * 54000, isozyme Tb3, about, sequence calculation, x * 79000, isozyme Tb4, about, sequence calculation Trypanosoma brucei
2.7.1.105 111000
-
 2 * 60000, recombinant Tb1, SDS-PAGE, 2 * 111000, isozyme Tb1, about, sequence calculation Trypanosoma brucei
2.7.1.105 140000
-
 recombinant isozyme Tb1, gel filtration Trypanosoma brucei
3.1.3.46 57078
-
 x * 57078, amino acid sequence calculation Trypanosoma brucei
3.1.3.46 140000
-
 isozyme 2, gel filtration Trypanosoma brucei
3.1.3.46 600000
-
 about, isozyme 1, gel filtration Trypanosoma brucei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.105 ATP + beta-D-fructose 6-phosphate Trypanosoma brucei
-
 ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 additional information Trypanosoma brucei evolution of the bifunctional enzyme ?
-
 ?
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O Trypanosoma brucei beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105 D-fructose 6-phosphate + phosphate
-
 ?
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O Trypanosoma cruzi beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105 D-fructose 6-phosphate + phosphate
-
 ?
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O Leishmania major beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105 D-fructose 6-phosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.105 Trypanosoma brucei Q52MQ5 stock 427, bifunctional enzyme, 4 isozymes
-
2.7.1.105 Trypanosoma brucei Q6PY95 stock 427
-
3.1.3.46 Leishmania major
-
-
-
3.1.3.46 Trypanosoma brucei
-
 stock 427, isozymes 1-4
-
3.1.3.46 Trypanosoma cruzi
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.105 from cytosol, 9000fold by ion exchange and affinity chromatography Trypanosoma brucei
2.7.1.105 native enzyme from stock 427 by ion exchange and affinity chromatography, recombinant His-tagged wild-type and mutant isozyme Tb1 from Escherichia coli Trypanosoma brucei
3.1.3.46 recombinant His-tagged isozymes 1-4 from purified trypomastigotes, by anion exchange and adsorption chromatography, ultrafiltration and dialysis Trypanosoma brucei

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.105 ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities, residues K51, T52, D128, and K172 are key catalytic residues for the 6-phosphofructo-2-kinase activity Trypanosoma brucei
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.46 trypomastigote bloodstream form, grown in rats Trypanosoma brucei
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.105 additional information
-
-
 Trypanosoma brucei
2.7.1.105 0.011
-
 purified enzyme Trypanosoma brucei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.105 ATP + beta-D-fructose 6-phosphate
-
 Trypanosoma brucei ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 ATP + beta-D-fructose 6-phosphate bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites Trypanosoma brucei ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 additional information evolution of the bifunctional enzyme Trypanosoma brucei ?
-
 ?
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105 Trypanosoma brucei D-fructose 6-phosphate + phosphate
-
 ?
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105 Trypanosoma cruzi D-fructose 6-phosphate + phosphate
-
 ?
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O beta-D-fructose 2,6-bisphosphate synthesis is catalyzed by the second enzyme activity 6-phosphofructo-2-kinase, EC 2.7.1.105 Leishmania major D-fructose 6-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.105 ? x * 72000, isozyme Tb2, about, sequence calculation, x * 54000, isozyme Tb3, about, sequence calculation, x * 79000, isozyme Tb4, about, sequence calculation Trypanosoma brucei
2.7.1.105 dimer 2 * 60000, recombinant Tb1, SDS-PAGE, 2 * 111000, isozyme Tb1, about, sequence calculation Trypanosoma brucei
2.7.1.105 More bifunctional enzyme domain structure, the bifunctional enzyme possesses a 6-phosphofructo-2-kinase and a fructose-2,6-bisphosphatase domain, as well as ankyrin-motif repeats, overview Trypanosoma brucei
3.1.3.46 ? x * 57078, amino acid sequence calculation Trypanosoma brucei
3.1.3.46 More evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview Trypanosoma brucei
3.1.3.46 More evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview Trypanosoma cruzi
3.1.3.46 More evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview Leishmania major

Synonyms

EC Number Synonyms Comment Organism
2.7.1.105 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
 Trypanosoma brucei
2.7.1.105 Pfk-2
-
 Trypanosoma brucei
2.7.1.105 PFK-2/FBPase-2
-
 Trypanosoma brucei
3.1.3.46 fructose-2,6-bisphosphatase
-
 Trypanosoma brucei
3.1.3.46 fructose-2,6-bisphosphatase
-
 Trypanosoma cruzi
3.1.3.46 fructose-2,6-bisphosphatase
-
 Leishmania major
3.1.3.46 More bifunctional enzyme, cf. EC 2.7.1.105 Trypanosoma brucei
3.1.3.46 More bifunctional enzyme, cf. EC 2.7.1.105 Trypanosoma cruzi
3.1.3.46 More bifunctional enzyme, cf. EC 2.7.1.105 Leishmania major
3.1.3.46 PFK-2/FBPase-2
-
 Trypanosoma brucei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.105 30
-
 assay at Trypanosoma brucei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.105 6
-
 about Trypanosoma brucei
2.7.1.105 7.1
-
 assay at Trypanosoma brucei

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.105 ATP
-
 Trypanosoma brucei
2.7.1.105 ATP binding site of isozyme Tb1, overview Trypanosoma brucei

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.105 0.7
-
 phosphoenolpyruvate 30°C Trypanosoma brucei

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.1.105 Trypanosoma brucei isozymes, sequence calculation
-
 9.3
3.1.3.46 Trypanosoma brucei amino acid sequence calculation
-
 9.29