Substrate specificities of wild- and mutated-type farnesyl diphosphate synthases with artificial substrate homologs
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- Nagaki Masahiko
- Graduate School of Science and Technology, Hirosaki University
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- Miyata Kazuhiko
- Graduate School of Science and Technology, Hirosaki University
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- Kawakami Jun
- Graduate School of Science and Technology, Hirosaki University
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- Miyamoto Ryo
- Graduate School of Science and Technology, Hirosaki University
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- Maki Yuji
- Department of Material and Biological Chemistry, Faculty of Science, Yamagata University
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- Sagami Hiroshi
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
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- Koyama Tanetoshi
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
抄録
6,7-Epoxygeranyl diphosphate was examined for reactivity as an allylic substrate of wild and mutated farnesyl diphosphate (FPP) synthases of Bacillus stearothermophilus. 6,7-Epoxygeranyl diphosphate was accepted by wild and mutated (Y81R, Y81D, and Y81S) farnesyl diphosphate synthases as a substrate in reaction with isopentenyl diphosphate, yielding 10,11-epoxyfarnesyl and 14,15-epoxygeranylgeranyl diphosphates, respectively.
収録刊行物
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- Transactions of the Materials Research Society of Japan
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Transactions of the Materials Research Society of Japan 34 (3), 533-536, 2009
一般社団法人 日本MRS
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詳細情報 詳細情報について
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- CRID
- 1390282680490363008
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- NII論文ID
- 130005004039
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- COI
- 1:CAS:528:DC%2BD1MXhsFKktbzP
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- ISSN
- 21881650
- 13823469
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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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- 抄録ライセンスフラグ
- 使用不可