Title | Flux through the tetrahydrodipicolinate succinylase pathway is dispensable for L-lysine production in Corynebacterium glutamicum. |
Publication Type | Journal Article |
Year of Publication | 1999 |
Authors | Shaw-Reid, CA, McCormick, MM, Sinskey, AJ, Stephanopoulos, G |
Journal | Appl Microbiol Biotechnol |
Volume | 51 |
Issue | 3 |
Pagination | 325-33 |
Date Published | 1999 Mar |
ISSN | 0175-7598 |
Keywords | Acyltransferases, Amidohydrolases, Amino Acid Oxidoreductases, Corynebacterium, Glucose, Lysine, Mutagenesis, Time Factors, Transformation, Bacterial |
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. |
DOI | 10.1007/s002530051398 |
Alternate Journal | Appl Microbiol Biotechnol |
Citation Key | 240 |
PubMed ID | 10222581 |