Kinetic analysis of PPi-dependent phosphofructokinase from Porphyromonas gingivalis.
We have previously cloned the gene encoding a pyrophosphate-dependent phosphofructokinase (PFK), designated PgPFK, from Porphyromonas gingivalis, an oral anaerobic bacterium implicated in advanced periodontal disease. In this study, recombinant PgPFK was purified to homogeneity, and biochemically characterized. The apparent K(m) value for fructose 6-phosphate was 2.2 mM, which was approximately 20 times higher than that for fructose 1,6-bisphosphate. The value was significantly greater than any other described PFKs, except for Amycolatopsis methanolica PFK which is proposed to function as a fructose 1,6 bisphosphatase (FBPase). The PgPFK appears to serves as FBPase in this organism. We postulate that this may lead to the gluconeogenic pathways to synthesize the lipopolysaccharides and/or glycoconjugates essential for cell viability.
Arimoto
Takafumi
T
Department of Preventive Dentistry, Kyushu Dental College, Kitakyushu 803-8580, Japan.
Ansai
Toshihiro
T
Yu
Weixian
W
Turner
Anthony J
AJ
Takehara
Tadamichi
T
D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D010770:Phosphotransferases / Q000235:genetics / Q000378:metabolism*; D016966:Porphyromonas gingivalis / Q000201:enzymology*; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
D011994:Recombinant Proteins; D010770:Phosphotransferases; C022502:pyrophosphate-fructose 6-phosphate 1-phosphotransferase