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Literature summary for 3.1.3.11 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)

Cloned (Comment) Organism
expression in Escherichia coli Sus scrofa

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

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

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Subunits

Subunits Comment Organism
homotetramer
-
Sus scrofa

Turnover Number [1/s]

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

Ki Value [mM]

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