Výsledky vyhledávání - "Manuel Hofmann"

Akademický článek

On the nature of thiamine triphosphate in Arabidopsis

Autor: Manuel Hofmann, Sylvain Loubéry, Teresa B. Fitzpatrick

Publikováno v: Plant Direct, Vol 4, Iss 8, Pp n/a-n/a (2020)

Abstract Vitamin B1 is a family of molecules, the most renowned member of which is diphosphorylated thiamine (TDP)—a coenzyme vital for the activity of key enzymes of energy metabolism. Triphosphorylated thiamine derivatives also exist within this

Externí odkaz: https://doaj.org/article/263de0e9f1db40949c65f5ceeb000250

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Structural and functional insight into the plant unique multimodular triphosphosphate tunnel metalloenzymes of Arabidopsis thaliana

Autor: Marta Pesquera, Jacobo Martinez, Kai Wang, Manuel Hofmann, Sylvain Loubéry, Priscille Steensma, Michael Hothorn, Teresa B. Fitzpatrick

Triphosphate tunnel metalloenzymes (TTMs) are found in all biological kingdoms and have been characterized in microorganisms and animals. Members of the TTM family already characterized have divergent biological functions and act on a range of tripho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e0c3759b6db6e92674d855aecb48c6da
https://doi.org/10.1101/2022.03.18.484887

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Structural and functional studies of Arabidopsis thaliana triphosphate tunnel metalloenzymes reveal roles for additional domains

Autor: Marta Pesquera, Jacobo Martinez, Benoît Maillot, Kai Wang, Manuel Hofmann, Pierre Raia, Sylvain Loubéry, Priscille Steensma, Michael Hothorn, Teresa B. Fitzpatrick

Publikováno v: The Journal of biological chemistry. 298(11)

Triphosphate tunnel metalloenzymes (TTMs) are found in all biological kingdoms and have been characterized in microorganisms and animals. Members of the TTM family have divergent biological functions and act on a range of triphosphorylated substrates

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbfff6faf977ab2b600d2bad2286aaf5
https://pubmed.ncbi.nlm.nih.gov/36049521

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Chemoselective Dimerization of Phosphates

Autor: Alexandre Hofer, Michael O. Hottiger, Sara Jordi, Thérésa Bridget Fitzpatrick, Sarah-Kirsten N Gatter, Nicole Kieliger, Elia Marques, Henning J. Jessen, Elena Ferrari, Manuel Hofmann

Publikováno v: Organic Letters
Organic Letters, Vol. 18, No 13 (2016) pp. 3222-3225

A methodology for the synthesis of oligophosphate conjugates using phosphordiamidites is described. This strategy facilitates the straightforward preparation of C2-symmetric dinucleoside tri-, penta-, and heptaphosphates. Moreover, unsymmetric compou

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Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis

Autor: Francel W.A. Verstappen, Ottoline Leyser, Tatsiana Charnikhova, Binne Zwanenburg, Jo Hepworth, Aalt D. J. van Dijk, Steven M. Smith, Yanxia Zhang, Harro J. Bouwmeester, Carolien Ruyter-Spira, Manuel Hofmann, Sander van der Krol, Salim Al-Babili, Gavin R. Flematti, Adrian Scaffidi

Publikováno v: Nature Chemical Biology, 10, 1028-1033
Nature Chemical Biology, 10, 12, pp. 1028
Nature Chemical Biology 10 (2014)
Nature Chemical Biology, 10, 1028

Strigolactones (SLs) are a class of phytohormones and rhizosphere signaling compounds with high structural diversity. Three enzymes, carotenoid isomerase DWARF27 and carotenoid cleavage dioxygenases CCD7 and CCD8, were previously shown to convert all

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d41632924c2a8d8f11aedd3b8c8e2812
https://pubmed.ncbi.nlm.nih.gov/25344813

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On the substrate- and stereospecificity of the plant carotenoid cleavage dioxygenase 7

Autor: Adrian Alder, Manuel Hofmann, Salim Al-Babili, Mark Bruno, Peter Beyer, Martina Vermathen

Publikováno v: FEBS letters. 588(9)

Strigolactones are phytohormones synthesized from carotenoids via a stereospecific pathway involving the carotenoid cleavage dioxygenases 7 (CCD7) and 8. CCD7 cleaves 9-cis-β-carotene to form a supposedly 9-cis-configured β-apo-10′-carotenal. CCD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f51c9deb5ca1f3a03eb39412b7c47f15
https://pubmed.ncbi.nlm.nih.gov/24685691

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