Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Chemical Compound Review:

AC1NT1A0 (5R)-8-methyl-8- azabicyclo[3.2.1]octan-3-one

Synonyms:

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Tropinone

Sixteen chimeric TR enzymes were expressed in Escherichia coli, and their stereospecificities, substrate specificities, and Km values for tropinone were compared with those of the wild-type enzymes [1].
Tropine dehydrogenase was induced by growth of Pseudomonas AT3 on atropine, tropine or tropinone [2].

High impact information on Tropinone

In the synthesis of tropane alkaloids in several medicinal plants, the TRs reduce a carbonyl group of an alkaloid intermediate, tropinone, to hydroxy groups with different diastereomeric configurations [3].
A modeling study indicated that these charged residues play a major role in controlling the binding orientation of tropinone within the substrate binding site, thereby determining the stereospecificity of the reaction product [3].
Tropinone reductase-II (TR-II) catalyzes the NADPH-dependent reduction of the carbonyl group of tropinone to a beta-hydroxyl group [4].
Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis [4].
The recombinant TRII protein expressed in Escherichia coli catalyzes pseudotropine formation from tropinone with a Km value, a pH optimum, substrate and co-substrate preferences similar to those reported for the TRII enzymes from other Solanaceae species [5].

Biological context of Tropinone

Putative tropinone reductase sequences annotated in plant genomes other that Solanaceae await functional characterisation [6].
Both tropinone reductases are NADPH-dependent short-chain dehydrogenases with amino acid sequence similarity of more than 50% suggesting their descent from a common ancestor [6].
Insight into the molecular evolution of two tropinone reductases [7].

Gene context of Tropinone

Molecular cloning, expression and characterization of tropinone reductase II, an enzyme of the SDR family in Solanum tuberosum (L.) [5].
Km values for the physiological substrate tropinone are 1.30 mM (TR I) and 0.11 mM (TR II) [8].

Analytical, diagnostic and therapeutic context of Tropinone

Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases [9].
Crystallization and preliminary crystallographic study of tropinone reductase II from Datura stramonium [10].

References

Opposite stereospecificity of two tropinone reductases is conferred by the substrate-binding sites. Nakajima, K., Hashimoto, T., Yamada, Y. J. Biol. Chem. (1994) [Pubmed]
Tropine dehydrogenase: purification, some properties and an evaluation of its role in the bacterial metabolism of tropine. Bartholomew, B.A., Smith, M.J., Long, M.T., Darcy, P.J., Trudgill, P.W., Hopper, D.J. Biochem. J. (1995) [Pubmed]
Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold. Nakajima, K., Yamashita, A., Akama, H., Nakatsu, T., Kato, H., Hashimoto, T., Oda, J., Yamada, Y. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis. Yamashita, A., Kato, H., Wakatsuki, S., Tomizaki, T., Nakatsu, T., Nakajima, K., Hashimoto, T., Yamada, Y., Oda, J. Biochemistry (1999) [Pubmed]
Molecular cloning, expression and characterization of tropinone reductase II, an enzyme of the SDR family in Solanum tuberosum (L.). Keiner, R., Kaiser, H., Nakajima, K., Hashimoto, T., Dräger, B. Plant Mol. Biol. (2002) [Pubmed]
Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Dräger, B. Phytochemistry (2006) [Pubmed]
Insight into the molecular evolution of two tropinone reductases. Nakajima, K., Oshita, Y., Yamada, Y., Hashimoto, T. Biosci. Biotechnol. Biochem. (1999) [Pubmed]
The reduction of tropinone in Datura stramonium root cultures by two specific reductases. Portsteffen, A., Dräger, B., Nahrstedt, A. Phytochemistry (1994) [Pubmed]
Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases. Nakajima, K., Kato, H., Oda, J., Yamada, Y., Hashimoto, T. J. Biol. Chem. (1999) [Pubmed]
Crystallization and preliminary crystallographic study of tropinone reductase II from Datura stramonium. Yamashita, A., Nakajima, K., Kato, H., Hashimoto, T., Yamada, Y., Oda, J. Acta Crystallogr. D Biol. Crystallogr. (1998) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.