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Literature summary for 2.7.1.105 extracted from

  • Pyko, M.; Rider, M.H.; Hue, L.; Wegener, G.
    6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase from frog skeletal muscle: purification, kinetics and immunological properties (1993), J. Comp. Physiol. B, 163, 89-98.
    View publication on PubMed
Search for more literature for 2.7.1.105

Inhibitors

Inhibitors Comment Organism Structure
citrate strong Pelophylax lessonae
additional information no inhibition by phosphorylation with Ca2+/calmodulin dependent protein kinase; no inhibition by protein kinase C Pelophylax lessonae
phosphoenolpyruvate strong Pelophylax lessonae
sn-glycerol 3-phosphate not Pelophylax lessonae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53900
-
 2 * 53900, muscle-type isozyme, SDS-PAGE Pelophylax lessonae
55800
-
 2 * 55800, liver isoenzyme, SDS-PAGE Pelophylax lessonae

Organism

Organism UniProt Comment Textmining
Pelophylax lessonae
-
 frog
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein
-
 Pelophylax lessonae

Purification (Commentary)

Purification (Comment) Organism
2 isozymes, liver (L) and muscle (M) type Pelophylax lessonae

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 55800, liver isoenzyme, SDS-PAGE Pelophylax lessonae
dimer 2 * 53900, muscle-type isozyme, SDS-PAGE Pelophylax lessonae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.3
-
 muscle-type isozyme Pelophylax lessonae