Abstract
AbstractL‐lysine synthesis pathway enzyme activities: β‐aspartate kinase (EC.2.7.2.4), diaminopimelate decarboxylase (EC.4.1.1.20) for two L‐lysine producing strains Brevibacterium flavum 22LD and RC‐115 were studied. It has been found that β‐aspartate kinase and diaminopimelate decarboxylase in the Br. flavum RC‐115 are less sensitive to feed‐back inhibition by lysine and threonine. It is supposed that desensitized β‐aspartate kinase in the Br. flavum RC‐115 can be determined by genetical changes of the regulatory properties of the β‐aspartate kinase.Auxotrophity in the locus of homoserine dehydrogenase was tested and no homoserine dehydrogenase (EC.1.1.1.3) activity was found in either strain.The combination of these both types of mutation supplemented by the lack of catabolic repression in the RC‐115 strain makes it an active lysine producer in the medium with high carbohydrates content.
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