The pyruvate dehydrogenase complex of Corynebacterium glutamicum: an attractive target for metabolic engineering.
The pyruvate dehydrogenase complex (PDHC) catalyzes the oxidative thiamine pyrophosphate-dependent decarboxylation of pyruvate to acetyl-CoA and CO2. Since pyruvate is a key metabolite of the central metabolism and also the precursor for several relevant biotechnological products, metabolic engineering of this multienzyme complex is a promising strategy to improve microbial production processes. This review summarizes the current knowledge and achievements on metabolic engineering approaches to tailor the PDHC of Corynebacterium glutamicum for the bio-based production of l-valine, 2-ketosiovalerate, pyruvate, succinate and isobutanol and to improve l-lysine production.
Institute of Microbiology and Biotechnology, University of Ulm, 89069 Ulm, Germany.
Bernhard J
BJ
Eikmanns
Institute of Biochemical Engineering, University of Stuttgart, 70569 Stuttgart, Germany. Electronic address: blombach@ibvt.uni-stuttgart.de.
Bastian
B
Blombach
D000440:Butanols; D048230:Corynebacterium glutamicum / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D060847:Metabolic Engineering; D011768:Pyruvate Dehydrogenase Complex; D019289:Pyruvic Acid; D014633:Valine
D000440:Butanols; D011768:Pyruvate Dehydrogenase Complex; C040507:isobutyl alcohol; D019289:Pyruvic Acid; D014633:Valine
Amino and organic acid production; Corynebacterium glutamicum; Isobutanol production; Metabolic engineering; Pyruvate dehydrogenase complex