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Literature summary for 3.1.3.46 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)

Cloned (Comment) Organism
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
DNA and amino acid sequence determination and analysis, phylogenetic analysis Trypanosoma cruzi
DNA and amino acid sequence determination and analysis, phylogenetic analysis Leishmania major

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis Trypanosoma brucei
additional information
-
additional information kinetic analysis Trypanosoma cruzi
additional information
-
additional information kinetic analysis Leishmania major

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57078
-
x * 57078, amino acid sequence calculation Trypanosoma brucei
140000
-
isozyme 2, gel filtration Trypanosoma brucei
600000
-
about, isozyme 1, gel filtration Trypanosoma brucei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
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
-
?
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

Organism UniProt Comment Textmining
Leishmania major
-
-
-
Trypanosoma brucei
-
stock 427, isozymes 1-4
-
Trypanosoma cruzi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged isozymes 1-4 from purified trypomastigotes, by anion exchange and adsorption chromatography, ultrafiltration and dialysis Trypanosoma brucei

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
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

Subunits Comment Organism
? x * 57078, amino acid sequence calculation Trypanosoma brucei
More evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview Trypanosoma brucei
More evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview Trypanosoma cruzi
More evolution of the bifunctional enzyme structure and organization, conserved motifs in the N-terminal region, e.g. ankyrin motifs, overview Leishmania major

Synonyms

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

pI Value

Organism Comment pI Value Maximum pI Value
Trypanosoma brucei amino acid sequence calculation
-
9.29