Zobrazeno 1 - 10
of 239
pro vyhledávání: '"Orotidine 5'-phosphate decarboxylase"'
Autor:
Kreuter, Johanna
Aureobasidium pullulans ist ein polymorpher hefeähnlicher Ascomycet, der in verschiedensten Lebensräumen und unter verschiedensten Umweltbedingungen zu finden ist. Er wird vorwiegend als Biokontrollmittel in der Landwirtschaft und zur industriellen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c0990e1b3a45efd05b8579c547e971f
Publikováno v:
Journal of biotechnology. 325
Claviceps purpurea is a filamentous fungus well known as a widespread plant pathogen, but it is also an important ergot alkaloid producer exploited by the pharmaceutic industry. In this work, we demonstrated that CRISPR/Cas9 can be a tool for directe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9f958b40b9b57141e955c0954cd91fb
https://pubmed.ncbi.nlm.nih.gov/33053363
https://pubmed.ncbi.nlm.nih.gov/33053363
Publikováno v:
Mycoscience. 58:35-39
To reduce the unnecessary gene clusters in the taxol-producing fungus Pestalotiopsis microspora, we report the development of an effective DNA deletion method that relies on a deletion cassette constructed with the Gateway-technique and overlap exten
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9ca611aaa394c76ab860863d8cd25c38
https://doi.org/10.1016/j.myc.2016.08.003
https://doi.org/10.1016/j.myc.2016.08.003
Akademický článek
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Autor:
Mahmoud Kandeel, Abdulla Al-Taher
Publikováno v:
Journal of Camel Practice and Research. 27:81
In this study, the metabolic pathways and the enzymes involved in uridine 5’-monophosphate (UMP) were investigated in camel and the blood parasite Trypanosoma evansi (T. evansi). The pyrimidine pathway of T. evansi was found to be devoid of uridine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5cb132b71c1d835aaaea47b5223964b3
https://doi.org/10.5958/2277-8934.2020.00012.0
https://doi.org/10.5958/2277-8934.2020.00012.0
Publikováno v:
Chemical Engineering Science. 134:504-509
Uridine 5′-monophosphate synthesis by orotidine 5′-phosphate decarboxylase was modeled taking into account a detailed reaction pathway and formation of all possible intermediates. Contributions from zwitterion mechanism, covalent mechanism, carbe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ce5235232d811aa585f25e109fb681f5
https://doi.org/10.1016/j.ces.2015.05.048
https://doi.org/10.1016/j.ces.2015.05.048
Publikováno v:
Engineering in Life Sciences. 15:542-549
Pestalotiopsis microspora NK17 produces the antitumor drug paclitaxel and pestalotiollide B, an analog of cholesterol ester transfer protein inhibitors. However, little is known about their biosynthesis due to the lack of molecular tools. We report h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04f58312d66547bbcba8a2fe80f37723
https://doi.org/10.1002/elsc.201400220
https://doi.org/10.1002/elsc.201400220
Akademický článek
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Publikováno v:
Journal of the American Chemical Society
The mechanism for activation of orotidine 5'-monophosphate decarboxylase (OMPDC) by interactions of side chains from Gln215 and Try217 at a gripper loop and R235, adjacent to this loop, with the phosphodianion of OMP was probed by determining the kin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73344c67582c1679ca29095f62fc963c
http://europepmc.org/articles/PMC4227808
http://europepmc.org/articles/PMC4227808
Autor:
Masahiro Fujihashi, Lakshmi P. Kotra, Kunio Miki, Toyokazu Ishida, Shingo Kuroda, Emil F. Pai
Publikováno v:
Journal of the American Chemical Society. 135:17432-17443
Orotidine 5'-monophosphate decarboxylase (ODCase) accelerates the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) by 17 orders of magnitude. Eight new crystal structures with ligand analogues combined with comput
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea22fae719782ac1c3e6f692ae43bb64
https://doi.org/10.1021/ja408197k
https://doi.org/10.1021/ja408197k