Characterization of the Aspartate Family Amino Acids Biosynthetic Enzymes in<scp>L</scp>-Threonine- and<scp>L</scp>-Lysine-producing Mutants of<i>Methylobacillus glycogens</i>
書誌事項
- タイトル別名
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- Characterization of the Aspartate Family Amino Acids Biosynthetic Enzymes in L-Threonine- and L-Lysine-producing Mutants of Methylobacillus glycogenes.
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Several enzymes involved in the L-threonine and L-lysine biosynthesis in gram-negative obligate methylotrophs, Methylobacillus glycogenes ATCC 21276 and ATCC 21371, were characterized. The activities of aspartokinases were inhibited by L-threonine or L-lysine. The homoserine dehydrogenases were inhibited by L-threonine or L-phenylalanine. The dihydrodipicolinate synthase activities were inhibited by L-lysine. No activity of meso-α, ε-dihydrodipicolinate dehydrogenase, the by-path enzyme of L-lysine biosynthesis, was detected. The biosynthetic enzymes in L-threonine-producing and L-lysine-producing mutants of M. glycogenes were also characterized. The aspartokinases of all the mutants were insensitive to inhibition by L-threonine, and some were also insensitive to inhibition by L-lysine. The homoserine dehydrogenases of the mutants had the wild type-profiles. The dihydrodipicolinate synthase of the L-lysine-producing mutant was partially desensitized to inhibition by L-lysine.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 57 (3), 461-466, 1993
公益社団法人 日本農芸化学会
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詳細情報
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- CRID
- 1390282681447460224
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- NII論文ID
- 110002676250
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DyaK3sXktVeksL0%3D
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- ISSN
- 13476947
- 09168451
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- 本文言語コード
- en
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- データソース種別
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- JaLC
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- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可