Open AccessBiochemical characterization of an active pyrophosphate‐dependent phosphofructokinase from Treponema pallidum
Author(s) -
Roberson Russell S,
Ronimus Ron S,
Gephard Susanne,
Morgan Hugh W
Publication year - 2001
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.1574-6968.2001.tb09479.x
Subject(s) - phosphofructokinase , pyrophosphate , allosteric regulation , treponema , chemistry , biochemistry , enzyme , active site , dimer , biology , glycolysis , organic chemistry , syphilis , human immunodeficiency virus (hiv) , immunology
An active pyrophosphate‐dependent phosphofructokinase containing a six residue polyhistidine tag has been cloned from Treponema pallidum , and characterized biochemically. The phosphofructokinase has pH optima for activity of 8.0 for both the forward and reverse reactions. The apparent K m for pyrophosphate was 0.042 mM ( V max of 141 U mg −1 protein) and for fructose‐6‐phosphate, 0.529 mM. The apparent K m for the reverse reaction for fructose‐1,6‐diphosphate was 0.267 mM ( V max of 42.4 U mg −1 protein). The enzyme appears to be both a dimer and non‐allosteric.