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.
Department of Biological Chemistry, University of Health Sciences, Chicago Medical School, Illinois 60064.
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Kemp
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Tripathi
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