Characterization of the pyrophosphate-dependent 6-phosphofructokinase from Methylococcus capsulatus Bath.

@article{Reshetnikov2008CharacterizationOT,
  title={Characterization of the pyrophosphate-dependent 6-phosphofructokinase from Methylococcus capsulatus Bath.},
  author={Alexander S. Reshetnikov and Olga N. Rozova and Valentina N. Khmelenina and Ildar I. Mustakhimov and Alexander P Beschastny and John Colin Murrell and Yuri Aleksandrovich Trotsenko},
  journal={FEMS microbiology letters},
  year={2008},
  volume={288 2},
  pages={202-10}
}
An active pyrophosphate-dependent 6-phosphofructokinase (PPi-PFK) from the thermotolerant methanotroph Methylococcus capsulatus Bath, containing a six-residue polyhistidine tag, was characterized. The enzyme was homodimeric (2 x 45 kDa), nonallosteric and most active at pH 7.0. PPi-PFK catalyzed reactions of PPi-dependent phosphorylation of fructose-6-phosphate (F-6-P) (K(m) 2.27 mM and V(max) 7.6 U mg(-1) of protein), sedoheptulose-7-phosphate (K(m) 0.027 mM and V(max) 31 U mg(-1)) and… CONTINUE READING

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