Title : Study of the roles of Arg-104 and Arg-225 in the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase by site-directed mutagenesis.

Pub. Date : 1995 Jul 1

PMID : 7619077






8 Functional Relationships(s)
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Protein Name
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1 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus
2 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus
3 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus
4 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus
5 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus
6 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus
7 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus
8 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 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 Rattus norvegicus