Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Julia Kufka"'
Autor:
Ludger Wessjohann, Svetlana Zakharova, Diana Schulze, Julia Kufka, Roman Weber, Lars Bräuer, Wolfgang Brandt
Publikováno v:
CHIMIA, Vol 63, Iss 6 (2009)
The functional role of isoprenoids and especially enzymatic prenylation in nature and human application is briefly covered, with the focus on bioinformatical, mechanistical and structural aspects of prenyltransferases and terpene synthases. These enz
Externí odkaz:
https://doaj.org/article/ed9b9cd9bbb64e1d9cedcf4ced2424d9
Publikováno v:
BIOspektrum
Late stage enzymatic prenylation and methylation are means to diversify (natural) compounds and to specify their functions. In eukaryotes and microbes, these steps are performed by large enzyme families, the prenyl and methyl transferases, which modi
Publikováno v:
Journal of Cheminformatics
Prenyltransfering enzymes are at the basis of the vast isoprenoid natural product diversity. 4-Hydroxybenzoate oligoprenyltransferase of E. coli, encoded in the gene ubiA, is a key enzyme in the biosynthetic pathway to ubiquinone. No X-ray structure
Autor:
Felix Rausch, Ludger A. Wessjohann, Eva Schulze, Wolfgang Brandt, Roman Weber, Nils Guennewich, Julia Kufka, Lars Braeuer, Svetlana Zakharova, Diana Schulze
Publikováno v:
ChemInform. 41
Autor:
Diana Schulze, Roman Weber, Ludger A. Wessjohann, Wolfgang Brandt, Lars Bräuer, Julia Kufka, Svetlana Zakharova
Publikováno v:
CHIMIA, Vol 63, Iss 6 (2009)
The functional role of isoprenoids and especially enzymatic prenylation in nature and human application is briefly covered, with the focus on bioinformatical, mechanistical and structural aspects of prenyltransferases and terpene synthases. These enz
Autor:
Eva Schulze, Wolfgang Brandt, Nils Günnewich, Julia Kufka, Diana Schulze, Svetlana Zakharova, Lars Bräuer, Ludger A. Wessjohann, Felix Rausch, Roman Weber
Publikováno v:
Phytochemistry. 70(15-16)
General thermodynamic calculations using the semiempiric PM3 method have led to the conclusion that prenyldiphosphate converting enzymes require at least one divalent metal cation for the activation and cleavage of the diphosphate-prenyl ester bond,