Mutagenesis of charged residues in a conserved sequence in the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

Arg-136, Glu-137, Arg-138 and Arg-139 are conserved in all sequences of the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Their role was studied by site-directed mutagenesis. All the mutations had little, if any, effect on fructose-2,6-bisphosphatase activity. Mutations of...

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Veröffentlicht in:	Biochemical journal 1997-02, Vol.321 ( Pt 3) (3), p.609-614
Hauptverfasser:	Bertrand, L, Vertommen, D, Feytmans, E, Di Pietro, A, Rider, M H, Hue, L
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acid Sequence Animals Biochemistry, Molecular Biology Circular Dichroism Conserved Sequence - genetics Fluorescence Fructose-Bisphosphatase - chemistry Fructose-Bisphosphatase - metabolism Fructosephosphates - metabolism Guanidine Guanidines - pharmacology Isoenzymes - metabolism Kinetics Life Sciences Models, Chemical Molecular Sequence Data Mutagenesis, Site-Directed - genetics Mutation - genetics Oligodeoxyribonucleotides - chemistry Oligodeoxyribonucleotides - genetics Phosphofructokinase-1 - chemistry Phosphofructokinase-1 - metabolism Phosphofructokinase-2 Phosphotransferases (Alcohol Group Acceptor) - chemistry Phosphotransferases (Alcohol Group Acceptor) - metabolism Protein Binding Protein Denaturation Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Alignment
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