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Literature summary for 2.7.1.105 extracted from

  • Garcia de Frutos, P.; Baanante, I.V.
    The muscle isoform of 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase of the teleost Sparus aurata: relationship with the liver isoform (1995), Arch. Biochem. Biophys., 321, 297-302.
    View publication on PubMed
Search for more literature for 2.7.1.105

Inhibitors

Inhibitors Comment Organism Structure
citrate
-
 Sparus aurata
additional information phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not skeletal muscle enzyme Sparus aurata
phosphoenolpyruvate
-
 Sparus aurata
sn-glycerol 3-phosphate most potent inhibitor of phosphorylated liver enzyme, phosphorylation enhances sensitivity; skeletal muscle enzyme is not sensitive to inhibition Sparus aurata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.21
-
 beta-D-fructose 2,6-bisphosphate pH 7.4, 30°C, in presence of phosphate Sparus aurata
0.223
-
 ATP pH 7.4, 30°C, presence of phosphate Sparus aurata
0.94
-
 beta-D-fructose 6-phosphate pH 7.4, 30°C, presence of phosphate Sparus aurata

Organism

Organism UniProt Comment Textmining
Sparus aurata
-
 teleost fish
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not skeletal muscle enzyme Sparus aurata

Purification (Commentary)

Purification (Comment) Organism
skeletal muscle Sparus aurata

Reaction

Reaction Comment Organism Reaction ID
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46 Sparus aurata
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Sparus aurata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + beta-D-fructose 6-phosphate
-
 Sparus aurata ADP + beta-D-fructose 2,6-bisphosphate
-
 r
additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Sparus aurata ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Sparus aurata

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.12
-
 citrate pH 7.4, 30°C Sparus aurata
0.23
-
 phosphoenolpyruvate pH 7.4, 30°C Sparus aurata