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Literature summary for 3.1.3.11 extracted from

  • Villeret, V.; Huang, S.; Zhang, Y.; Lipscomb, W.N.
    Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography (1995), Biochemistry, 34, 4307-4315.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the enzyme complexed with AMP, the substrate analogue 2,5-anhydro-D-glucitol 1,6-diphosphosphate and Mn2+ Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
AMP structural aspects of the allosteric inhibition Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-diphosphate + H2O
-
Sus scrofa D-fructose 6-phosphate + phosphate
-
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