Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Patrick Rabe"'
Publikováno v:
Angewandte Chemie International Edition. 57:3238-3241
Two bacterial diterpene synthases from the actinomycete Allokutzneria albata were investigated, resulting in the identification of the structurally unprecedented compound spiroalbatene from the first and cembrene A from the second enzyme. Both enzyme
Publikováno v:
Chemistry - A European Journal. 23:10501-10505
Two diterpene cyclases, one from the social amoeba Dictyostelium discoideum and the other from the bacterium Streptomyces clavuligerus, with products containing a Z-configured double bond between the original C2 and C3 of geranylgeranyl diphosphate,
Autor:
Etilia Dolja, Patrick Rabe, Jan Rinkel, Britta Nubbemeyer, Jeroen S. Dickschat, T. Hoang Luu, Thomas Schmitz
Publikováno v:
Angewandte Chemie International Edition. 56:2776-2779
The mechanisms of two diterpene cyclases from streptomycetes-one with an unknown product that was identified as the spirocyclic hydrocarbon spiroviolene and one with the known product tsukubadiene-were investigated in detail by isotope labeling exper
Publikováno v:
Organic & Biomolecular Chemistry. 15:2353-2358
Genome sequencing of Streptomyces malaysiensis DSM 4137 revealed the presence of four terpene cyclase genes, one of which was characterised as (+)-isoafricanol synthase. Its cyclisation mechanism was extensively studied using isotopically labelled pr
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 12, Iss 1, Pp 2317-2324 (2016)
The stereochemical course of the cyclisation reaction catalysed by the bacterial 1,8-cineol synthase from Streptomyces clavuligerus was investigated using stereospecifically deuterated substrates. In contrast to the well investigated plant enzyme fro
Autor:
Patrick Rabe, Jeroen S. Dickschat
Publikováno v:
Beilstein Journal of Organic Chemistry
Beilstein Journal of Organic Chemistry, Vol 12, Iss 1, Pp 1380-1394 (2016)
Beilstein Journal of Organic Chemistry, Vol 12, Iss 1, Pp 1380-1394 (2016)
Farnesyl diphosphate (FPP) and all fifteen positional isomers of (13C1)FPP were enzymatically converted by the bacterial terpene cyclases corvol ether synthase from Kitasatospora setae, the epi-cubebol synthase from Streptosporangium roseum, and the
Autor:
Aron Janusko, Ramona Riclea, Patrick Rabe, Christian A. Citron, Jeroen S. Dickschat, Jan Rinkel, Tim A. Klapschinski, Lena Barra
Publikováno v:
Angewandte Chemie International Edition. 54:13448-13451
An uncharacterized terpene cyclase from Streptomyces pratensis was identified as (+)-(1(10)E,4E,6S,7R)-germacradien-6-ol synthase. The enzyme product exists as two interconvertible conformers, resulting in complex NMR spectra. For the complete assign
Structures and Biosynthesis of Corvol Ethers-Sesquiterpenes from the ActinomyceteKitasatospora setae
Publikováno v:
Angewandte Chemie International Edition. 54:6041-6045
Here we present the functional characterization of a sesquiterpene cyclase from Kitasatospora setae. The enzyme converts the sesquiterpene precursor farnesyl diphosphate (FPP) into two previously unknown and unstable sesquiterpene ethers for which we
Autor:
Lena Barra, Christian A. Citron, Patrick Rabe, Tsutomu Hoshino, Chiaki Nakano, Jeroen S. Dickschat
Publikováno v:
European Journal of Organic Chemistry. 2014:7684-7691
A flexible, efficient and robust method for the synthesis of isotopically labelled oligoprenyl diphosphates was developed. The method makes use of just a few building blocks (acetone, triethyl phosphonoacetate, and ethyl acetoacetate) from which seve
Autor:
Harro J. Bouwmeester, Jeroen S. Dickschat, Arman Beyraghdar Kashkooli, Jan Rinkel, Patrick Rabe
Publikováno v:
Beilstein Journal of Organic Chemistry, 13, 1770-1780. Beilstein-Institut Zur Forderung der Chemischen Wissenschaften
Beilstein Journal of Organic Chemistry, 13, 1770-1780
Beilstein Journal of Organic Chemistry 13 (2017)
Beilstein Journal of Organic Chemistry, Vol 13, Iss 1, Pp 1770-1780 (2017)
Beilstein Journal of Organic Chemistry, 13, 1770-1780
Beilstein Journal of Organic Chemistry 13 (2017)
Beilstein Journal of Organic Chemistry, Vol 13, Iss 1, Pp 1770-1780 (2017)
The product obtained in vitro from a diterpene synthase encoded in the genome of the bacterium Chitinophaga pinensis, an enzyme previously reported to have germacrene A synthase activity during heterologous expression in Escherichia coli, was identif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2412b32a93de92c89346766f4ef83157
https://dare.uva.nl/personal/pure/en/publications/18hydroxydolabella37diene-synthase--a-diterpene-synthase-from-chitinophaga-pinensis(edc384c8-1055-44d2-acf1-34667a7c8063).html
https://dare.uva.nl/personal/pure/en/publications/18hydroxydolabella37diene-synthase--a-diterpene-synthase-from-chitinophaga-pinensis(edc384c8-1055-44d2-acf1-34667a7c8063).html