Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Balaikaite A"'
Autor:
Stephen A. Marshall, Karl A. P. Payne, Karl Fisher, Mark D. White, Aisling Ní Cheallaigh, Arune Balaikaite, Stephen E. J. Rigby, David Leys
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
The UbiD-UbiX decarboxylase system is required for the biosynthesis of quinone cofactors. Here, the authors combine structural and biochemical analyses to elucidate the UbiX reaction mechanism, showing that it resembles the mode of action of class I
Externí odkaz:
https://doaj.org/article/7d6536e8acd943bea50c5023037c7730
Publikováno v:
In The Enzymes 2020 47:517-549
Autor:
Karl A. P. Payne, Arune Balaikaite, Karl Fisher, Stephen A. Marshall, A. Ni Cheallaigh, White, Stephen E. J. Rigby, David Leys
Publikováno v:
Nature Communications
Marshall, S, Payne, K, Fisher, K, White, M, Ni Cheallaigh, A, Balaikaite, A, Rigby, S & Leys, D 2019, ' The UbiX flavin prenyltransferase reaction mechanism resembles Class I terpene cyclase chemistry ', Nature Communications . https://doi.org/10.1038/s41467-019-10220-1
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Marshall, S, Payne, K, Fisher, K, White, M, Ni Cheallaigh, A, Balaikaite, A, Rigby, S & Leys, D 2019, ' The UbiX flavin prenyltransferase reaction mechanism resembles Class I terpene cyclase chemistry ', Nature Communications . https://doi.org/10.1038/s41467-019-10220-1
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
The UbiX-UbiD enzymes are widespread in microbes, acting in concert to decarboxylate alpha-beta unsaturated carboxylic acids using a highly modified flavin cofactor, prenylated FMN (prFMN). UbiX serves as the flavin prenyltransferase, extending the i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65f7dcb904686f65d2d1b5d793a4f413
Publikováno v:
ACS Chemical Biology
Prenylated flavin mononucleotide (prFMN) is a recently discovered modified flavin cofactor containing an additional nonaromatic ring, connected to the N5 and C6 atoms. This cofactor underpins reversible decarboxylation catalyzed by members of the wid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce4b4cf36df0805d89f7bb26264950ab
Autor:
Marshall, Stephen A., Payne, Karl A.P., Fisher, Karl, Gahloth, Deepankar, Bailey, Samuel S., Balaikaite, Arune, Saaret, Annica, Gostimskaya, Irina, Aleku, Godwin, Huang, Huanming, Rigby, Stephen E.J., Procter, David, Leys, David *
Publikováno v:
In Methods in Enzymology 2019 620:489-508
Akademický článek
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Autor:
Stephen A, Marshall, Karl A P, Payne, Karl, Fisher, Deepankar, Gahloth, Samuel S, Bailey, Arune, Balaikaite, Annica, Saaret, Irina, Gostimskaya, Godwin, Aleku, Huanming, Huang, Stephen E J, Rigby, David, Procter, David, Leys
Publikováno v:
Methods in enzymology. 620
The recent discovery of the prenylated FMN (prFMN) cofactor has led to a renewed interest in the prFMN-dependent UbiD family of enzymes. The latter catalyses the reversible decarboxylation of alpha-beta unsaturated carboxylic acids and features widel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::078794f67c40e7afa73e102f1241ef1f
https://pubmed.ncbi.nlm.nih.gov/31072499
https://pubmed.ncbi.nlm.nih.gov/31072499
Autor:
Huan-Ming Huang, David J. Procter, Godwin A. Aleku, Arune Balaikaite, Annica Saaret, Stephen E. J. Rigby, Irina Gostimskaya, Karl A. P. Payne, David Leys, Karl Fisher, Samuel S. Bailey, Stephen A. Marshall, Deepankar Gahloth
The recent discovery of the prenylated FMN (prFMN) cofactor has led to a renewed interest in the prFMN-dependent UbiD family of enzymes. The latter catalyses the reversible decarboxylation of alpha-beta unsaturated carboxylic acids and features widel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::228a1fb4edd16998ea10c817d65ecc15
https://doi.org/10.1016/bs.mie.2019.03.022
https://doi.org/10.1016/bs.mie.2019.03.022
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Saaret A; Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester, United Kingdom., Balaikaite A; Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester, United Kingdom., Leys D; Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester, United Kingdom. Electronic address: david.leys@manchester.ac.uk.
Publikováno v:
The Enzymes [Enzymes] 2020; Vol. 47, pp. 517-549. Date of Electronic Publication: 2020 Jul 18.