Literature summary for 2.7.1.11 extracted from

Marinho-Carvalho, M.M.; Zancan, P.; Sola-Penna, M.
Modulation of 6-phosphofructo-1-kinase oligomeric equilibrium by calmodulin: formation of active dimers (2006), Mol. Genet. Metab., 87, 253-261.

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Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
skeletal muscle	-	Oryctolagus cuniculus	-

Subunits

Subunits	Comment	Organism
tetramer	binding of calmodulin to the high affinity site of 6-phosphofructo-1-kinase induces dimerization of the enzyme, but does not inhibit the catalytic activity. Dissociation of the enzyme tetramers induced by calmodulin occurs under very low concentrations of the Ca2+-binding protein and requires Ca2+	Oryctolagus cuniculus

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Release 2023.1 (January 2023)