- 著者
- 高橋 宣治 内田 健一 中川 彰 松崎 桂一 大村 智 中村 朝朗 三宅 洋子 武 佳和 甲斐荘 正恒
- 出版者
- 天然有機化合物討論会実行委員会
- 雑誌
- 天然有機化合物討論会講演要旨集
- 巻号頁・発行日
- vol.35, pp.762-768, 1993
The biosynthesis of lactacystin, a new microbial metabolite which induces differentiation of neuroblastoma cells, was studied by ^<13>C NMR spectroscopy using various ^<13>C labeled precursors. The feeding experiment of L-[2-^<13>C ] leucine showed a strong enrichement at C-5 of Lactacystin. Incorporation of [1-^<13>C] isobutyrate labeled C-1, C-4, C-8, and C-14. These ^<13>C labeling patterns indicate that lactacystin consists of three biosynthetic units, namely isobutyrate (or L-valine), L-leucine, and L-cysteine. The C_<10> unit containing γ-lactam moiety arises by a condensation between methylmalonate semialdehyde and C-5 of the C_6 unit derived biosynthetically from L-leucine, followed by intramolecular cyclization. The stereochemistry of two diastereotopic methyl carbons of lactacystin which appeard at δc 19.85 and δc 21.37 was investigated by incorporation of a new type of chiral ^<13>C L-leucine (or L-valine), designated as the ^<13>C block labeled leucine (or valine), which was obtained from the fermentation of leucine producing organism using a mixture of 99% [U-^<13>C_6] glucose and natural glucose as a carbon source.
1 0 0 0 OA ミオシンホスファターゼ阻害タンパク質 CPI-17の構造と機能
- 著者
- 大木 進野 江藤 真澄 松澤 史子 甲斐荘 正恒
- 出版者
- 一般社団法人 日本生物物理学会
- 雑誌
- 生物物理 (ISSN:05824052)
- 巻号頁・発行日
- vol.45, no.2, pp.72-77, 2005 (Released:2005-03-25)
- 参考文献数
- 17
Cell motility, including smooth muscle contraction and cell migration, is regulated by reversible phosphorylation of myosin. Recent studies have shown that myosin phosphatase (MP), along with kinases, contributes dynamically to the regulation of myosin-II phosphorylation. An MP specific inhibitor named CPI-17, which is expressed in smooth muscle and neuronal cells, mediates receptor signaling leading to myosin-II phosphorylation. In this review, we discuss structure/function relationships of CPI-17 stemming from our recent NMR studies and computer modeling results. The combination of biophysical approaches with biochemical techniques has revealed the inhibitory mechanism of CPI-17.