Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site-Reference-Cited by-同舟云学术

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Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site

Published:2016-05-10 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Sayer Christopher,Finnigan William,Isupov Michail N.,Levisson Mark,Kengen Servé W. M.,van der Oost John,Harmer Nicholas J.,Littlechild Jennifer A.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep25542.pdf

Reference60 articles.

1. Klenk, H. P. et al. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390, 364–370 (1997).

2. Littlechild, J. A. et al. Natural methods of protein stabilization: thermostable biocatalysts. Biochem Soc Trans 35, 1558–1563 (2007).

3. Littlechild, J. A. Enzymes from extreme environments and their industrial applications. Front Bioeng Biotechnol 3, 161 (2015).

4. Levisson, M., van der Oost, J. & Kengen, S. W. M. Carboxylic ester hydrolases from hyperthermophiles. Extremophiles 13, 567–581 (2009).

5. Romano, D. et al. Esterases as stereoselective biocatalysts. Biotechnol Adv 33, 547–565 (2015).

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