Open AccessKinetic analysis of PPi‐dependent phosphofructokinase from Porphyromonas gingivalis
Author(s) -
Arimoto Takafumi,
Ansai Toshihiro,
Yu Weixian,
Turner Anthony J.,
Takehara Tadamichi
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11024.x
Subject(s) - porphyromonas gingivalis , phosphofructokinase , microbiology and biotechnology , chemistry , bacteroidaceae , biology , bacteria , biochemistry , enzyme , glycolysis , genetics
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.