Abstract
A 3.2 kb chromosomal DNA fragment encoding homoserine dehydrogenase (HD) of Brevibacterium lactofermentum M-15, a l-threonine and l-lysine producing mutant, was cloned into the unique Pstl site of vector plasmid pAJ1844. Strain M-15 was transformed with the obtained recombinant plasmid pAJ210. The transformant, AJ12021, showed 2-fold higher HD activity and accumulated a 1.4-fold higher amount of l-threonine (maximally 25.0 g/liter) than in the case of the host strain, M-15, respectively. The correlation between the amino acid production and the regulation of enzyme activities was discussed.
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