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   <subfield code="a">Molecular breeding of a Brevibacterium lactofermentum l -phenylalanine producer using a cloned prephenate dehydratase gene</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Hisao Ito, Katsuaki Sato, Kazuhiko Matsui, Konosuke Sano, Hitoshi Enei, Yoshio Hirose]</subfield>
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   <subfield code="a">Summary: The prephenate dehydratase gene was cloned from a mutant of Brevibacterium lactofermentum, AJ11957 that produced enzyme free from feedback inhibition. The recombinant plasmids pPH11 and pPH14 complemented a phenylalanine auxotroph of B. lactofermentum, A-15, provided the transformant with the desensitized enzyme and caused an increased level of the enzyme compared to that of a wild strain. Plasmid pPH14 was introduced into l-phenylalanine producers genetically induced from B. lactofermentum; MF358 and FP-1 excreting l-tyrosine and anthranilate, respectively, as by-products. Both transformants predominantly accumulated l-phenylalanine at the expense of by-product formation. Co-existence of pPH14 and pTAR16, a recombinant plasmid expressing desensitized 3-deoxy-d-arabino-hepturosonate-7-phosphate synthase had a marked effect on further improvement in l-phenylalanine productivity, accompanied by an increase in the corresponding enzyme activity. The parent, MF358, accumulating 5.5 g/l l-phenylalanine, 6.8 g/l l-tyrosine and 0.3 g/l anthranilate turned into a potent l-phenylalanine producer producing 18.2 g/l l-phenylalanine and 1.0 g/l l-tyrosine by-product.</subfield>
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   <subfield code="u">Process Development Laboratory, Central Research Laboratories, Ajinomoto Co., Inc. Suzuki-cho, 210, Kawasaki-ku, Kawasaki-shi, Japan</subfield>
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