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Literature summary extracted from

  • Zhang, F.W.; Zhao, F.K.; Xu, G.J.
    Molecular cloning, expression and purification of muscle fructose-1,6-bisphosphatase from Zaocys dhumnades: the role of the N-terminal sequence in AMP activation at alkaline pH (2000), Biol. Chem., 381, 561-566.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.11 AMP 20% activation at 0.001-0.002 mM of AMP at alkaline pH, KM value of 0.00018 mM at pH 7.5, 30°C, recombinant enzyme Homo sapiens
3.1.3.11 AMP 4fold activation at pH 9.2 Ptyas dhumnades
3.1.3.11 K+
-
 Homo sapiens
3.1.3.11 K+
-
 Ptyas dhumnades

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.11 commentary Ptyas dhumnades

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.11 AMP
-
 Homo sapiens
3.1.3.11 AMP the AMP binding is mainly located in the N-terminal region Ptyas dhumnades
3.1.3.11 additional information not: AMP Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.0001
-
 D-fructose 1,6-bisphosphate pH 7.5, 30°C, wild-type enzyme Ptyas dhumnades
3.1.3.11 0.00011
-
 D-fructose 1,6-bisphosphate pH 7.5, 30°C, recombinant enzyme Ptyas dhumnades
3.1.3.11 0.00014
-
 D-fructose 1,6-bisphosphate pH 7.5, 30°C, chimeric enzyme Ptyas dhumnades

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.11 36000
-
 x * 36000, SDS-PAGE Ptyas dhumnades

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.11 D-fructose 1,6-bisphosphate + H2O Ptyas dhumnades enzyme is usually regarded as a regulatory enzyme of gluconeogenesis D-fructose 6-phosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Homo sapiens
-
-
-
3.1.3.11 Ptyas dhumnades
-
 snake
-
3.1.3.11 Rattus norvegicus
-
-
-
3.1.3.11 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.11 side-chain modification a chimeric enzyme is constructed where the amino terminal residues, 1-60, are derived from the rat liver enzyme Ptyas dhumnades

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.11 recombinant enzyme Ptyas dhumnades

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.11 kidney
-
 Sus scrofa
-
3.1.3.11 liver
-
 Homo sapiens
-
3.1.3.11 liver
-
 Rattus norvegicus
-
3.1.3.11 muscle
-
 Homo sapiens
-
3.1.3.11 muscle
-
 Ptyas dhumnades
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.11 D-fructose 1,6-bisphosphate + H2O
-
 Ptyas dhumnades D-fructose 6-phosphate + phosphate
-
 ?
3.1.3.11 D-fructose 1,6-bisphosphate + H2O enzyme is usually regarded as a regulatory enzyme of gluconeogenesis Ptyas dhumnades D-fructose 6-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.11 ? x * 36000, SDS-PAGE Ptyas dhumnades

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.11 0.0006
-
 AMP pH 7.5, 30°C, recombinant enzyme Homo sapiens
3.1.3.11 0.0006
-
 AMP pH 7.5, 30°C, wild-type enzyme Ptyas dhumnades
3.1.3.11 0.00085
-
 AMP pH 7.5, 30°C, recombinant enzyme Ptyas dhumnades
3.1.3.11 1.2
-
 AMP pH 7.5, 30°C, chimeric enzyme Ptyas dhumnades