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Literature summary for 3.1.3.11 extracted from

  • Toyoda, Y.; Sy, J.
    Purification and phosphorylation of fructose-1,6-bisphosphatase from Kluyveromyces fragilis (1984), J. Biol. Chem., 259, 8718-8723.
    View publication on PubMed
Search for more literature for 3.1.3.11

Inhibitors

Inhibitors Comment Organism Structure
AMP
-
 Kluyveromyces marxianus
fructose 2,6-diphosphate
-
 Kluyveromyces marxianus
additional information rapid regulation of frucose-1,6-diphosphatase following glucose addition is controlled mainly by enzyme inhibitors Kluyveromyces marxianus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 4 * 35000, SDS-PAGE Kluyveromyces marxianus
155000
-
 sucrose density gradient centrifugation Kluyveromyces marxianus

Organism

Organism UniProt Comment Textmining
Kluyveromyces marxianus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification in absence of inhibitor, the enzyme is slowly phosphorylated with a maximum incorporation of 1 mol of phosphate per mol of enzyme. The presence of the inhibitors AMP and fructose 2,6-diphosphate greatly increases the phosphorylation rate with a maximum incorporation of 2 mol phosphate per mol of enzyme Kluyveromyces marxianus

Purification (Commentary)

Purification (Comment) Organism
-
 Kluyveromyces marxianus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
36
-
-
 Kluyveromyces marxianus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-diphosphate + H2O
-
 Kluyveromyces marxianus D-fructose 6-phosphate + phosphate
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 35000, SDS-PAGE Kluyveromyces marxianus