Dihydroxyacid dehydratase is important for gametophyte development and disruption causes increased susceptibility to salinity stress in Arabidopsis

Autor: Zhang, Chun, Pang, Qiuying, Jiang, Luguang, Wang, Shoucai, Yan, Xiufeng, Chen, Sixue, He, Yan

Publikováno v: Journal of Experimental Botany, 2015 Jan 01. 66(3), 879-888.

Externí odkaz: https://www.jstor.org/stable/26389941

The active site of the Mycobacterium tuberculosis branched-chain amino acid biosynthesis enzyme dihydroxyacid dehydratase contains a 2Fe–2S cluster

Autor: Bashiri, Ghader, Grove, Tyler L., Hegde, Subray S., Lagautriere, Thomas, Gerfen, Gary J., Almo, Steven C., Squire, Christopher J., Blanchard, John S., Baker, Edward N.

Publikováno v: In Journal of Biological Chemistry 30 August 2019 294(35):13158-13170

Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.

The Aspergillus fumigatus Dihydroxyacid Dehydratase Ilv3A/IlvC Is Required for Full Virulence.

Autor: Oliver, Jason D.¹, Kaye, Sarah J.¹, Tuckwell, Danny¹, Johns, Anna E.², Macdonald, Darel A.², Livermore, Joanne², Warn, Peter A.², Birch, Mike¹ mike.bromley@manchester.ac.uk, Bromley, Michael J.², Nielsen, Kirsten³

Publikováno v: PLoS ONE. Sep2012, Vol. 7 Issue 9, Special section p1-11. 11p.

Function and maturation of the Fe-S center in dihydroxyacid dehydratase from Arabidopsis

Autor: Nicolas Rouhier, Michael K. Johnson, Huanyao Gao, Tamanna Azam, Jérémy Couturier, Sajini Randeniya

Publikováno v: Journal of Biological Chemistry 12 (293), 4422-4433. (2018)
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (12), pp.4422-4433. ⟨10.1074/jbc.RA117.001592⟩

Dihydroxyacid dehydratase (DHAD) is the third enzyme required for branched-chain amino acid biosynthesis in bacteria, fungi, and plants. DHAD enzymes contain two distinct types of active-site Fe–S clusters. The best characterized examples are Esche

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36396f37522f5271aa67ee047699806e
http://prodinra.inra.fr/record/428858