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Literature summary for 3.1.3.11 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

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drops in vapor diffusion, crystals of FBPase with citrate and fructose 2,6-bisphosphate Escherichia coli
hanging drops in vapor diffusion, crystals of Zn2+/fructose 2,6-bisphosphate complex Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
AMP AMP and D-fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase Escherichia coli
AMP
-
Sus scrofa
D-fructose 2,6-bisphosphate AMP and fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase Escherichia coli
fructose 2,6-bisphosphate global conformational change in porcine FBPase induced by fructose 2,6-bisphosphate in the absence of AMP Sus scrofa

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A993
-
-
Sus scrofa P00636
-
-

Synonyms

Synonyms Comment Organism
type I FBPase
-
Escherichia coli