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Literature summary extracted from

  • Nelson, S.W.; Honzatko, R.B.; Fromm, H.J.
    Hybrid tetramers of porcine liver fructose-1,6-bisphosphatase reveal multiple pathways of allosteric inhibition (2002), J. Biol. Chem., 277, 15539-15545.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.11 expression in Escherichia coli Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.11 AMP comparison of inhibition of homotetramer and hybrid tetramers Sus scrofa
3.1.3.11 D-fructose-2,6-bisphosphate two pathways of allosteric inhibition are possible Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.0018
-
 D-fructose-1,6-bisphosphate pH 7.5, 22°C, wild-type enzyme Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.11 additional information formation of hybrid tetramers and comparison of kinetic parameters Sus scrofa

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.11
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.11 liver
-
 Sus scrofa
-

Subunits

EC Number Subunits Comment Organism
3.1.3.11 homotetramer
-
 Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.11 22
-
 D-fructose-1,6-bisphosphate pH 7.5, 22°C, wild-type enzyme Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.11 0.00012
-
 D-fructose-2,6-bisphosphate pH 7.5, 22°C, wild-type enzyme Sus scrofa