z-logo
open-access-imgOpen Access
Pyrophosphate-dependent phosphofructo-1-kinase complements fructose 1,6-bisphosphatase but not phosphofructokinase deficiency in Escherichia coli
Author(s) -
Robert G. Kemp,
Rakesh Tripathi
Publication year - 1993
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.175.17.5723-5724.1993
Subject(s) - biology , escherichia coli , phosphofructokinase 2 , phosphofructokinase , biochemistry , propionibacterium freudenreichii , fructose 2,6 bisphosphate , fructose 1,6 bisphosphatase , enzyme , phosphofructokinase 1 , kinase , pyrophosphate , microbiology and biotechnology , glycolysis , gene , fermentation
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here