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Literature summary extracted from

  • Hines, J.K.; Chen, X.; Nix, J.C.; Fromm, H.J.; Honzatko, R.B.
    Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition (2007), J. Biol. Chem., 282, 36121-36131.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.46 as selenomethionine-substituted protein Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.11 hanging drops in vapor diffusion, crystals of FBPase with citrate and fructose 2,6-bisphosphate Escherichia coli
3.1.3.11 hanging drops in vapor diffusion, crystals of Zn2+/fructose 2,6-bisphosphate complex Sus scrofa
3.1.3.46 as hanging drops in vapor diffusion VDX plates in complex with Mg2+ or Zn2+ and beta-D-fructose 2,6-bisphosphate Sus scrofa
3.1.3.46 as hanging drops in vapor diffusion VDX plates with Mg2+, citrate and beta-D-fructose 2,6-bisphosphate Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.11 AMP AMP and D-fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase Escherichia coli
3.1.3.11 AMP
-
Sus scrofa
3.1.3.11 D-fructose 2,6-bisphosphate AMP and fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase Escherichia coli
3.1.3.11 fructose 2,6-bisphosphate global conformational change in porcine FBPase induced by fructose 2,6-bisphosphate in the absence of AMP Sus scrofa
3.1.3.46 AMP beta-D-fructose 2,6-bisphosphate has no effect on AMP inhibition Escherichia coli
3.1.3.46 AMP beta-D-fructose 2,6-bisphosphate enhances AMP inhibition Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Escherichia coli P0A993
-
-
3.1.3.11 Sus scrofa P00636
-
-
3.1.3.46 Escherichia coli
-
-
-
3.1.3.46 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.46 by Cibacron Blue-Sepharose and Sephadex G-50 column chromatography Escherichia coli
3.1.3.46 by Cibacron Blue-Sepharose and Sephadex G-50 column chromatography Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate beta-D-fructose 2,6-bisphosphate induces a global conformational change in the absence of AMP Sus scrofa
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate the complex of E. coli FBPase with beta-D-fructose 2,6-bisphosphate remains in the R-state with dynamic loops in the engaged conformation Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O
-
Escherichia coli D-fructose 6-phosphate + phosphate
-
?
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O
-
Sus scrofa D-fructose 6-phosphate + phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.11 type I FBPase
-
Escherichia coli
3.1.3.46 6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
Escherichia coli
3.1.3.46 6-phosphofructo-2-kinase/fructose-2 6-biphosphatase
-
Sus scrofa
3.1.3.46 FBPase
-
Escherichia coli
3.1.3.46 FBPase
-
Sus scrofa