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Difference between Enzymatic and Chemical N-methylations of Protoberberine-Type Alkaloid, Dependent on the Stereoisomer of (-)-N-methyl-7,8,13,13a-tetrahydroberberinium Salt.
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- Kamigauchi Miyoko
- Department of Physical Chemistry, Kobe Pharmaceutical University
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- Yoshida Mayumi
- Department of Physical Chemistry, Kobe Pharmaceutical University
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- Noda Yuko
- Department of Physical Chemistry, Kobe Pharmaceutical University
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- Nishijo Jujiro
- Department of Physical Chemistry, Kobe Pharmaceutical University
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- In Yasuko
- Osaka University of Pharmaceutical Sciences
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- Tomoo Koji
- Osaka University of Pharmaceutical Sciences
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- Ohishi Hirofumi
- Osaka University of Pharmaceutical Sciences
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- Ishida Toshimasa
- Osaka University of Pharmaceutical Sciences
Bibliographic Information
- Other Title
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- Difference between Enzymatic and Chemical N-methylations of Protoberberine-Type Alkaloid, Dependent on the Stereoisomer of (−)-<i>N</i>-methyl-7,8,13,13a-tetrahydroberberinium Salt
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Description
A possible relation between the stereostructure of (−)-(13aS)-tetrahydroberberine (1) and its enzymatic/chemical N-methylation, an important biosynthetic reaction to isoquinoline alkaloids in plants, was examined by CD spectroscopic, X-ray crystallographic, and energy calculation methods. The CD measurements indicated that 1 has two conformers (cis and trans) concerning the ring junction of the quinolizidine skeleton, and exist with a cis/trans ratio of about 1/4 in a diethyl ether : 2-methylbutane : ethanol (5 : 5 : 2) mixture. The dimensional/conformational difference between these cis and trans conformers was clarified by the X-ray crystal-structure analyses of two stereoisomers of N-methylated 1 (3 and 4). By using these structural parameters, the progress of N-methylation was simulated by energy profile calculations, suggesting that the cis and trans conformers are the major substrate for the enzymatic and chemical N-methylation reactions, respectively. Taking these results and the simulation of N-methylation of 1 by S-adenosyl-L-methionine at the binding pocket of N-methyltransferase into consideration, different pathways for chemical and enzymatic N-methylations of 1 have been proposed.
Journal
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- Bulletin of the Chemical Society of Japan
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Bulletin of the Chemical Society of Japan 76 (3), 587-593, 2003
The Chemical Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679096799616
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- NII Article ID
- 130004151422
- 80015784145
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- NII Book ID
- AA00580132
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- ISSN
- 13480634
- 00092673
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- NDL BIB ID
- 6474433
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed