(44). On the basis of this assay, the parallel function of the succinylase and acetylase variants supposed to operate in corynebacteria (16,44). The situation is even more complex, since the distribution of label from 14C-aspartate (23) and '3C-glucose (14,49) found in secreted * Corresponding author. lysine is inconsistent with the sole function of the succinylase or acetylase variant but requires operation of the dehydrogenase pathway, too. This resulted in the demonstration of diaminopimelate dehydrogenase activity in C. glutamicum, and it was concluded that all three variants could be used in parallel in this organism (16).Recently, the genes converting aspartate to lysine via the dehydrogenase variant have been cloned from C. glutamicum (7,14,18,51). During this cloning, a dapD mutant of E. coli devoid of PDC-N-succinyltransferase activity was also used (15,50
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