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Stimulation of glucose catabolism through the pentose pathway by the absence of the two pyruvate kinase isoenzymes in Escherichia coli
Author(s) -
Ponce Elizabeth,
Martínez Alfredo,
Bolívar Francisco,
Valle Fernando
Publication year - 1998
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19980420)58:2/3<292::aid-bit25>3.0.co;2-d
Subject(s) - pentose phosphate pathway , pyruvate kinase , biochemistry , catabolism , escherichia coli , mutant , phosphogluconate dehydrogenase , metabolism , kinase , strain (injury) , enzyme , isozyme , biology , glycolysis , chemistry , dehydrogenase , glucose 6 phosphate dehydrogenase , gene , anatomy
Escherichia coli strains devoid of one or both of the two pyruvate kinase isoenzymes (PKA and PKF), were grown on minimal media in batch fermentations. The strain lacking both PKs showed a 28% decrease on its specific growth rate when compared to the wild type. However, protein and CO 2 yields did not change. Using radioactive 1‐C 14 glucose and collecting the CO 2 produced by the cultures, it was found that the mutant lacking both pyruvate kinases, metabolized glucose mainly through the pentose pathway (PP). The increased participation of the PP in glucose metabolism in this strain, was also reflected on the levels of the glucose‐6‐phosphate and 6‐phosphogluconate dehydrogenases.© 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:292–295, 1998.