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Metabolic flux distributions in Corynebacterium glutamicum during growth and lysine overproduction
Author(s) -
Vallino Joseph J.,
Stephanopoulos Gregory
Publication year - 1993
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/bit.260410606
Subject(s) - corynebacterium glutamicum , biochemistry , lysine , metabolic flux analysis , overproduction , flux (metallurgy) , pentose phosphate pathway , metabolic network , fermentation , glyoxylate cycle , flux balance analysis , metabolic engineering , biosynthesis , pyruvate carboxylase , phosphoenolpyruvate carboxylase , phosphoenolpyruvate carboxykinase , biology , catabolite repression , metabolic pathway , chemistry , metabolism , amino acid , glycolysis , enzyme , organic chemistry , gene , mutant
The two main contributions of this are the solidification of Corynebacterium glutamicum biochemistry guided by bioreaction network analysis, and the determination of bansal metabolic flux distributions during growth and lysine synthesis. Employed methodology makes use of stoichiometrically based mass balances to determine flux distributions in the C. glutamicum metabolic network. Presented are a brief description of the methodology, a through literature review of glutamic acid bacteria biochemistry, and specific results obtained through a combination of fermentation studies and analysis‐directed intracellular assays. The latter include the findings of the lack of activity of glyoxylate shunt, and that phosphoenolpyruvate carboxylase (PPC) is the only anaplerotic reaction expressed in C. glutamicum cultivated on glucose minimal media. Network simplifications afforded by the above findings facilitated the determination of metabolic flux distributions under a variety of culture conditions and led to the following conclusions. Both the pentose phosphate pathway and PPC support fluxes during growth and lysine overproduction branch point does not appear to limit lysine synthesis. © 1993 John Wiley & Sons, Inc.