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Background   Corynebacterium glutamicum  cg1790/ pgk  encodes an enzyme active as a 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) catalyzing phosphoryl transfer from 1,3-biphosphoglycerate (bPG) to ADP to yield 3-phosphoglycerate (3-PG) and ATP in substrate chain phosphorylation.    Results   C. glutamicum  3-phosphoglycerate kinase was purified to homogeneity from the soluble fraction of recombinant  E. coli . PGK His  was found to be active as a homodimer with molecular weight of 104 kDa. The enzyme preferred conditions of pH 7.0 to 7.4 and required Mg 2+  for its activity. PGK His  is thermo labile and it has shown maximal activity at 50–65°C. The maximal activity of PGK His  was estimated to be 220 and 150 U mg -1  with K M  values of 0.26 and 0.11 mM for 3-phosphoglycerate and ATP, respectively. A 3-phosphoglycerate kinase negative  C. glutamicum  strain  ∆pgk  was constructed and shown to lack the ability to grow under glycolytic or gluconeogenic conditions unless PGK was expressed from a plasmid to restore growth. When  pgk  was overexpressed in L-arginine and L-ornithine production strains the production increased by 8% and by 17.5%, respectively.    Conclusion  Unlike many bacterial PGKs,  C. glutamicum  PGK is active as a homodimer. PGK is essential for growth of  C. glutamicum  with carbon sources requiring glycolysis and gluconeogenesis. Competitive inhibition by ADP reveals the critical role of PGK in gluconeogenesis by energy charge.  Pgk  overexpression improved the productivity in L-arginine and L-ornithine production strains.

Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production