Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Gerd Mittelstädt"'
Autor:
Christin Radon, Gerd Mittelstädt, Benjamin R. Duffus, Jörg Bürger, Tobias Hartmann, Thorsten Mielke, Christian Teutloff, Silke Leimkühler, Petra Wendler
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Rhodobacter capsulatus NAD+ dependent formate dehydrogenase (RcFDH) is a molybdoenzyme that catalyses the reversible oxidation of formate to carbon dioxide, and is of interest for biotechnological applications. Here the authors present the cryo-EM st
Externí odkaz:
https://doaj.org/article/ee6fb5dae1e445018b0579d644893722
Publikováno v:
Biochemistry. 61:1883-1893
Enzyme-catalyzed hydrolysis is a fundamental chemical transformation involved in many essential metabolic processes. The enzyme 5'-methylthioadenosine/
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ca0ef9356364f3c16a8e48da814a7cb
https://doi.org/10.1021/acs.biochem.2c00351
https://doi.org/10.1021/acs.biochem.2c00351
Publikováno v:
Philosophical Transactions of the Royal Society B: Biological Sciences. 378
Anthranilate phosphoribosyltransferase catalyses the second reaction in the biosynthesis of tryptophan from chorismate in microorganisms and plants. The enzyme is homodimeric with the active site located in the hinge region between two domains. A ran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd960544947ad65eeb4708fd49460709
https://doi.org/10.1098/rstb.2022.0039
https://doi.org/10.1098/rstb.2022.0039
Autor:
Isabelle Montgomerie, Thomas W. Bird, Olga R. Palmer, Ngarangi C. Mason, Theresa E. Pankhurst, Blair Lawley, Leonor C. Hernández, Rhodri Harfoot, Astrid Authier-Hall, Danielle E. Anderson, Kerry L. Hilligan, Kaitlin H. Buick, Naasson M. Mbenza, Gerd Mittelstädt, Samara Maxwell, Shubhra Sinha, Joanna Kuang, Kanta Subbarao, Emily J. Parker, Alan Sher, Ian F. Hermans, James E. Ussher, Miguel E. Quiñones-Mateu, Davide Comoletti, Lisa M. Connor
Publikováno v:
iScience. 26:106256
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::566f669f68ea55d421658b5c1a9a169d
https://doi.org/10.1016/j.isci.2023.106256
https://doi.org/10.1016/j.isci.2023.106256
Autor:
Isabelle Stewart, Thomas W. Bird, Olga Rose Palmer, Ngarangi Claire Mason, Theresa Ellen Pankhurst, Blair Lawley, Leonor C. Hernández, Rhodri Harfoot, Astrid Authier-Hall, Kerry L. Hilligan, Kaitlin Buick, Naasson M. Mbenza, Gerd Mittelstädt, Samara Maxwell, Shubra Sinha, Joanna Kuang, Emily Parker, Alan Sher, Ian F. Hermans, James Ussher, Miguel E. Quiñones-Mateu, Davide Comoletti, Lisa M Connor, VAANZ Group
Publikováno v:
SSRN Electronic Journal.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::afc0bf65ea89fa61fd445bf9accd8a6f
https://doi.org/10.2139/ssrn.4233518
https://doi.org/10.2139/ssrn.4233518
Autor:
Silke Leimkühler, Petra Wendler, Benjamin R. Duffus, Jörg Bürger, Thorsten Mielke, Tobias Hartmann, Christian Teutloff, Christin Radon, Gerd Mittelstädt
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor composition, but structural information on these enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2b62ab6f961453be82b899d84cabd69
https://hdl.handle.net/21.11116/0000-0006-4E44-721.11116/0000-0006-4E46-5
https://hdl.handle.net/21.11116/0000-0006-4E44-721.11116/0000-0006-4E46-5
Autor:
Gerd Mittelstädt, Emma K. Livingstone, Wanting Jiao, Emily J. Parker, Gert-Jan Moggré, Ali Reza Nazmi
Publikováno v:
Biochemical Journal. 475:247-260
Adenosine triphosphate (ATP) phosphoribosyltransferase (ATP-PRT) catalyses the first committed step of histidine biosynthesis in plants and microorganisms. Two forms of ATP-PRT have been reported, which differ in their molecular architecture and mech
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a37e2c953b54bd73cb0b2687350a85cc
https://doi.org/10.1042/bcj20170762
https://doi.org/10.1042/bcj20170762
Hinge Twists and Population Shifts Deliver Regulated Catalysis for ATP-PRT in Histidine Biosynthesis
Publikováno v:
Biophys J
Allosteric regulation plays an important role in the control of metabolic flux in biosynthetic pathways. In microorganisms, many enzymes in these pathways adopt different strategies of allostery to allow the tuning of their activities in response to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e784395c32aa2368f7303dd3458c502
https://europepmc.org/articles/PMC6531924/
https://europepmc.org/articles/PMC6531924/
Publikováno v:
FEBS Letters. 590:2603-2610
ATP-phosphoribosyltransferase (ATP-PRT) catalyses the first step of histidine biosynthesis. Two different forms of ATP-PRT have been described; the homo-hexameric long form, and the hetero-octameric short form. Lactococcus lactis possesses the short
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fe390788081681a81f81386f33689d0
https://doi.org/10.1002/1873-3468.12277
https://doi.org/10.1002/1873-3468.12277
Publikováno v:
Protein Science. 25:1492-1506
Adenosine triphosphate phosphoribosyltransferase (ATP-PRT) catalyzes the first committed step of the histidine biosynthesis in plants and microorganisms. Here, we present the functional and structural characterization of the ATP-PRT from the pathogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b8f9bc4170cef882b1048fa5748d8ec
https://doi.org/10.1002/pro.2948
https://doi.org/10.1002/pro.2948