Pyrophosphate-dependent phosphofructo-1-kinase complements fructose 1,6-bisphosphatase but not phosphofructokinase deficiency in Escherichia coli.
The gene from Propionibacterium freudenreichii for PPi-dependent phosphofructo-1-kinase, an enzyme that is found in some bacteria, in a number of anaerobic protists, and in plants, complements the absence of fructose 1,6-bisphosphatase in Escherichia coli but does not complement the deficiency of the ATP-dependent phosphofructokinase.
Kemp
R G
RG
Department of Biological Chemistry, University of Health Sciences, Chicago Medical School, Illinois 60064.
Tripathi
R L
RL
D000255:Adenosine Triphosphate / Q000378:metabolism; D011756:Diphosphates / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006597:Fructose-Bisphosphatase / Q000235:genetics / Q000378:metabolism*; D005816:Genetic Complementation Test; D010732:Phosphofructokinase-1 / Q000235:genetics / Q000378:metabolism*; D011424:Propionibacterium / Q000201:enzymology / Q000235:genetics
D011756:Diphosphates; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1; C068652:1-phosphofructokinase; D006597:Fructose-Bisphosphatase