Flux through the tetrahydrodipicolinate succinylase pathway is dispensable for l-lysine production in Corynebacterium glutamicum |
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Authors: | C A Shaw-Reid M M McCormick A J Sinskey G Stephanopoulos |
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Institution: | (1) Department of Chemical Engineering, Room 56-469, Massachusetts Institute of Technology, Cambridge, MA 02139 USA Tel.: +1-617-253-4583 Fax: +1-617-253-3122, US;(2) Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, US |
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Abstract: | The N-succinyl-ll-diaminopimelate desuccinylase gene (dapE) in the four-step succinylase branch of the l-lysine biosynthetic pathway of Corynebacterium glutamicum was disrupted via marker-exchange mutagenesis to create a mutant strain that uses only the one-step meso-diaminopimelate dehydrogenase branch to overproduce lysine. This mutant strain grew and utilized glucose from minimal medium
at the same rate as the parental strain. In addition, the dapE
−
strain produced lysine at the same rate as its parent strain. Transformation of the parental and dapE
−
strains with the amplified meso-diaminopimelate dehydrogenase gene (ddh) on a plasmid did not affect lysine production in either strain, despite an eightfold amplification of the activity of the
enzyme. These results indicate that the four-step succinylase pathway is dispensable for lysine overproduction in shake-flask
culture. In addition, the one-step meso-diaminopimelate dehydrogenase pathway does not limit lysine flux in Corynebacterium under these conditions.
Received: 20 May 1998 / Received revision: 12 August 1998 / Accepted: 3 September 1998 |
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