Literature summary for 2.7.1.11 extracted from

Li, Y.; Rivera, D.; Ru, W.; Gunasekera, D.; Kemp, R.G.
Identification of allosteric sites in rabbit phosphofructo-1-kinase (1999), Biochemistry, 38, 16407-16412.

Search for more literature for 2.7.1.11

Activating Compound

Activating Compound	Comment	Organism	Structure
cAMP	0.1 mM, approx. 5fold activation	Oryctolagus cuniculus
D-fructose 2,6-bisphosphate	half-maximal activation at 0.0003 mM	Oryctolagus cuniculus

Protein Variants

Protein Variants	Comment	Organism
R481D	no alteration in nucleotide binding to inhibitory site, 50% inhibition at 0.4-0.7 mM ATP, 10% of wild-type PFK activation with 0.1 mM fructose 2,6-bisphosphate	Oryctolagus cuniculus
R481L	no alteration in nucleotide binding to inhibitory site, 50% inhibition at 0.4-0.7 mM ATP	Oryctolagus cuniculus
R48L	similar specific activity as wild-type, less sensitive to ATP inhibition, not inhibited by citrate and 3-phosphoglycerate	Oryctolagus cuniculus

Inhibitors

Inhibitors	Comment	Organism	Structure
3-phosphoglycerate	1.5-2.0 mM, 50% inhibition	Oryctolagus cuniculus
ATP	0.4 mM, 50% inhibition of PFK C	Oryctolagus cuniculus
citrate	50% inhibition below 0.25 mM	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	-	-

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Release 2023.1 (January 2023)