The pyruvate dehydrogenase complex of Corynebacterium glutamicum: an attractive target for metabolic engineering.

Bernhard J Eikmanns, Bastian Blombach

Journal: Journal of biotechnology 2015;192 Pt B():339-45

PMID: 24486441

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Abstract

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.

Address: Institute of Microbiology and Biotechnology, University of Ulm, 89069 Ulm, Germany.; Institute of Biochemical Engineering, University of Stuttgart, 70569 Stuttgart, Germany. Electronic address: [email protected].

DOI: 10.1016/j.jbiotec.2013.12.019

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MeSH Terms: Butanols, Corynebacterium glutamicum, Metabolic Engineering, Pyruvate Dehydrogenase Complex, Pyruvic Acid, Valine