| Autor: |
Kozhushkov, Sergei I., Zlatopolskiy, Boris D., Brandl, Melanie, Alvermann, Petra, Radzom, Markus, Geers, Bernardette, de Meijere, Armin, Zeeck, Axel |
| Zdroj: |
European Journal of Organic Chemistry; March 2005, Vol. 2005 Issue: 5 p854-863, 10p |
| Abstrakt: |
The deuterium-labeled racemic 3-(trans-2-nitrocyclopropyl)-alanine (rac-[D2]-3) and 3-(trans-2-aminocyclopropyl)alanine (rac-[D2]-4) as well as non-labeled rac-3-[trans-2-(hydroxycarbonyl)cyclopropyl]alanine (rac-5a) and rac-3-[trans-2-(methoxycarbonyl)cyclopropyl]alanine (rac-5b) were prepared in 43, 18, 88 and 49 % overall yield, respectively, along a general synthetic route applying alkylations of the lithium enolate of tert-butyl (diphenylmethylene)-aminoacetate (O’Donnel’s glycine equivalent 11) as a key step. Feeding experiments with these amino acids and Streptomyces griseoflavus (strain W 384) revealed that rac-[D2]-3, rac-5a and rac-5b are incorporated to give hormaomycin 1b and its analogue 23, respectively, while rac-[D2]-4 is not. Feeding of rac-2-(trans-2-nitrocyclopropyl)glycine (rac-6) unexpectedly gave the 5-nitronorvaline-containing hormaomycin analogues 25a–c. This is rationalized as arising from a cyclopropyl to homoallyl anion rearrangement followed by enzymatic hydrogenation of the double bond. These experiments provided new insights into the substrate specificity of the enzyme which assembles hormaomycin. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005) |
| Databáze: |
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