PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10727432-5	2000	WISK phosphorylated recombinant heart PFK-2 in a time-dependent manner to the extent of 0.4 mol of phosphate incorporated/mol of enzyme subunit, and increased the V(max) of PFK-2 twofold, without affecting the K(m) for fructose 6-phosphate.	fructose-6-phosphate	219-239	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	38-43	
9890979-2	1999	A bifunctional enzyme, fructose-6-phosphate,2-kinase/fructose 2, 6-bisphosphatase (Fru-6-P,2-kinase/Fru-2,6-Pase), catalyzes synthesis and degradation of fructose 2,6-bisphosphate (Fru-2,6-P2).	fructose-6-phosphate	83-90	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	23-81	
7619077-2	1995	In recombinant rat liver PFK-2/FBPase-2, mutation of Arg-225 to Ser increased the Km of PFK-2 for fructose-6-phosphate (Fru-6-P) 7-fold at pH 6 and decreased PFK-2 activity at suboptimal substrate concentrations between pH 6 and 9.5.	fructose-6-phosphate	98-118	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	25-30	
7619077-2	1995	In recombinant rat liver PFK-2/FBPase-2, mutation of Arg-225 to Ser increased the Km of PFK-2 for fructose-6-phosphate (Fru-6-P) 7-fold at pH 6 and decreased PFK-2 activity at suboptimal substrate concentrations between pH 6 and 9.5.	fructose-6-phosphate	98-118	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	88-93	
7619077-2	1995	In recombinant rat liver PFK-2/FBPase-2, mutation of Arg-225 to Ser increased the Km of PFK-2 for fructose-6-phosphate (Fru-6-P) 7-fold at pH 6 and decreased PFK-2 activity at suboptimal substrate concentrations between pH 6 and 9.5.	fructose-6-phosphate	98-118	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	88-93	
7619077-2	1995	In recombinant rat liver PFK-2/FBPase-2, mutation of Arg-225 to Ser increased the Km of PFK-2 for fructose-6-phosphate (Fru-6-P) 7-fold at pH 6 and decreased PFK-2 activity at suboptimal substrate concentrations between pH 6 and 9.5.	fructose-6-phosphate	120-127	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	25-30	
7619077-2	1995	In recombinant rat liver PFK-2/FBPase-2, mutation of Arg-225 to Ser increased the Km of PFK-2 for fructose-6-phosphate (Fru-6-P) 7-fold at pH 6 and decreased PFK-2 activity at suboptimal substrate concentrations between pH 6 and 9.5.	fructose-6-phosphate	120-127	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	88-93	
7619077-2	1995	In recombinant rat liver PFK-2/FBPase-2, mutation of Arg-225 to Ser increased the Km of PFK-2 for fructose-6-phosphate (Fru-6-P) 7-fold at pH 6 and decreased PFK-2 activity at suboptimal substrate concentrations between pH 6 and 9.5.	fructose-6-phosphate	120-127	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	88-93	
7619077-9	1995	In recombinant rat muscle PFK-2/FBPase-2, mutation of Arg-104 to Ser increased the Km for Fru-6-P 60-fold, increased the IC50 of citrate, increased the Vmax.	fructose-6-phosphate	90-97	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	26-31	
7619077-15	1995	The findings indicate that Arg-104 is involved in Fru-6-P binding in the PFK-2 domain and that it might also bind citrate.	fructose-6-phosphate	50-57	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2	Rattus norvegicus	73-78