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Literature summary for 3.1.3.11 extracted from

  • Noda, T.; Hoffschulte, H.; Holzer, H.
    Characterization of fructose 1,6-bisphosphatase from bakers yeast (1984), J. Biol. Chem., 259, 7191-7197.
    View publication on PubMed
Search for more literature for 3.1.3.11

Inhibitors

Inhibitors Comment Organism Structure
AMP
-
 Saccharomyces cerevisiae
fructose 2,6-diphosphate
-
 Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ divalent cation required. Mn2+ or Mg2+ Saccharomyces cerevisiae
Mn2+ divalent cation required. Mn2+ or Mg2+ Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
116000
-
 gel filtration Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification fructose 1,6-diphosphatase a is the active non-phosphorylated form of the enzyme. Fructose 1,6-diphosphatase b is the less active phosphorylated form of the enzyme Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
46.1
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9.5 pH 6.5: about 40% of maximal activity, pH 9.5: about 60% of maximal activity Saccharomyces cerevisiae