Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Elina, Siirola"'
Publikováno v:
JACS Au, Vol 3, Iss 5, Pp 1267-1283 (2023)
Externí odkaz:
https://doaj.org/article/96c373e92c964c98a992346dfddb4e62
Autor:
Elina Siirola, Fabian Eggimann, Charles Moore, Kirsten Schroer, Alexandra Vargas, Theo Peschke, Thierry Schlama, Radka Snajdrova
Publikováno v:
CHIMIA, Vol 77, Iss 6 (2023)
The fortieth anniversary of biocatalysis started at Ciba-Geigy and later at Novartis is a great time to pause and reflect on development of science and technology in this field. Enzyme-based synthesis became a highly valued enabling tool for pharmace
Externí odkaz:
https://doaj.org/article/3d30ebe868c74ebe81b48aa586696c7b
Akademický článek
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Autor:
Ahir Pushpanath, Elina Siirola, Antonio Zanotti-Gerosa, Amin Bornadel, Samantha Staniland, Serena Bisagni, Tommaso Angelini, Beatriz Dominguez
Publikováno v:
Johnson Matthey Technology Review. 64:529-536
The asymmetric reduction of C=C double bonds is a sought-after chemical transformation to obtain chiral molecules used in the synthesis of fine chemicals. Biocatalytic C=C double bond reduction is a particularly interesting transformation complementa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::375f2bf7cf66506ef0c5f7c82e6f3c65
https://doi.org/10.1595/205651320x16001815466116
https://doi.org/10.1595/205651320x16001815466116
Publikováno v:
ACS Catalysis. 7:3204-3209
The direct asymmetric reductive amination of ketones using ammonia as the sole amino donor is a growing field of research in both chemocatalysis and biocatalysis. Recent research has focused on the enzyme engineering of amino acid dehydrogenases (to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3ebc246e18bd59d270de42ce2734c149
https://doi.org/10.1021/acscatal.7b00516
https://doi.org/10.1021/acscatal.7b00516
Publikováno v:
Pharmaceutical Biocatalysis ISBN: 9780429353116
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30dd4a2fe5e4a26938b7cbd8c637a046
https://doi.org/10.1201/9780429353116-15
https://doi.org/10.1201/9780429353116-15
Publikováno v:
European Journal of Organic Chemistry. 2014:6753-6760
Burkholderia cepacia lipase (lipase PS-D) catalysed acylation with 3,3-difluoro-4-phenyl-, -thiophen-3-yl- and -4-pyridylazetidin-2-ones was examined for the formation of N-Boc-protected 6-O-acylated sugar–β-amino acid conjugates from methyl α-D-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7971faf8298bf4d638614535ad26456
https://doi.org/10.1002/ejoc.201402800
https://doi.org/10.1002/ejoc.201402800
Autor:
Wolfgang Kroutil, Elina Siirola
Publikováno v:
Topics in Catalysis. 57:392-400
Retro-Friedel–Crafts hydrolases are co-factor independent enzymes with unusual reactivity and selectivity. These unique hydrolases are scarcely studied for biocatalytical applications in organic chemistry yet, although many other hydrolytic enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dc5e2c9541d0cc8049ab6a01db2713f9
https://doi.org/10.1007/s11244-013-0193-0
https://doi.org/10.1007/s11244-013-0193-0
Publikováno v:
Topics in Catalysis. 57:376-384
Phloretin hydrolase from Eubacterium ramulus (Phy) catalyzes the hydrolysis of the dihydrochalcone phloretin to phloroglucinol and phloretic acid, performing a formal retro- Friedel–Crafts acylation reaction on its substrate. Its closest sequence h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6bec580e0b90426f4b02ac523fd65ce4
https://doi.org/10.1007/s11244-013-0196-x
https://doi.org/10.1007/s11244-013-0196-x
Publikováno v:
Advanced Synthesis & Catalysis. 355:1677-1691
Although CC bond hydrolases are distributed widely in Nature, they has as yet have received only limited attention in the area of biocatalysis compared to their counterpart the C-heteroatom hydrolases, such as lipases and proteases. However, the subs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd4ff0c7d28277e4c5667459d60ed9bf
https://doi.org/10.1002/adsc.201300232
https://doi.org/10.1002/adsc.201300232