Enzymatic alteration in the shikimate pathway during derivation of menaquinone-4-producing mutants of Flavobacterium sp. 238-7.
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- TAGUCHI Hisataka
- Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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- KITA Shunbun
- Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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- TANI Yoshiki
- Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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Activities of seven enzymes of the shikimate pathway were compared between the wild-type strain and menaquinone-4-producing mutant strains of Flavobacterium sp. 238-7. Activity of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthase, the first regulatory enzyme in the shikimate pathway, was almost the same in these strains in the stationary phase, but the activity of a sulfonamide-resistant strain, SP0736, was 2 times higher than that of other strains in the logarithmic phase. Shikimate dehydrogenase activity was almost the same among these strains during cultivation. Other enzyme activities of mutants were 1.5-4 fold higher than those of the wild-type strain. DAHP synthase and shikimate kinase were found to be inhibited by chorismate and MK-4. Feedback inhibition for shikimate kinase by chorismate was partially removed in strain SP0736.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 55 (3), 769-773, 1991
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
- 1390282681441794432
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- NII論文ID
- 110006325431
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- NII書誌ID
- AA00515312
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- ISSN
- 18811280
- 00021369
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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
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可