The enzymatic transformation of leaf-movement factor in Lespedeza cuneata G. Don controlled by a biological clock

Chemistry Letters

Volumn , Issue 2, 1998, Pages 179-180

  Ueda, Minoru ^a   Ohnuki, Takashi ^a   Yamamura, Shosuke ^a  

^a KEIO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0032378912     PISSN: 03667022     EISSN: None     Source Type: Journal    
DOI: 10.1246/cl.1998.179     Document Type: Article

References (12)

1. H. Schildknecht and K. Schumacher Pure Appl. Chem., 54, 2501 (1982).
2. H. Schildknecht, Angew. Chem. Int. Ed. Engl., 22, 695 (1983). and references cited therein.
3. E. Miyoshi, Y. Shizuri, and S. Yamamura, Chem. Lett., 1987, 511.
4. M. Ueda, M. Niwa, and S. Yamamura, Phytochemistry, 39, 817 (1995).
5. M. Ueda, T. Shigemori-Suzuki, and S. Yamamura, Tetrahedron Lett., 36, 6267 (1995).
6. H. Shigemori, N. Sakai, E. Miyoshi, Y. Shizuri, and S. Yamamura,Tetrahedron, 46, 383 (1990).
7. M. Ueda, T. Ohnuki, and S. Yamamura, Tetrahedron, Lett., 38, 2497 (1997).
8. M. Ueda, C. Tashiro, and S. Yamamura, Tetrahedron Lett., 38, 3253 (1997).
9. M. Ueda, T. Ohnuki, and S. Yamamura, submitted
10. The increase of 4 cannot be explained only by the hydrolysis of 2 and 3. But, 4 is known as one of the important intermediate of many secondary metabolites. We suppose that the increase of 4 is also affected by the control of other biosyhthetic pathways. In addition, There is another possibility that potassium O-D-glucopyranosyl-lespedezate and -isolespedezate, which will show much lower activity as described in ref. 6, coexist together with 2 and 3.
11. H. Watanabe, S. Watanabe, R. Nakajima, J-H. Moon, K. Shimokihara, J. Inagaki, H. Etoh, T. Asai, K. Sakata, and K. Ina, Biosci. Biotech. Biochem., 57, 1101 (1993).
12. The leaf-opening substance 2 used in the enzymatic transformation is transformed into a mixture of 2 and 3 at room temperature on the reaction (see ref. 6).