Directed evolution of prenylated FMN-dependent Fdc supports efficient in vivo isobutene production

Autor: Annica Saaret, Benoît Villiers, François Stricher, Macha Anissimova, Mélodie Cadillon, Reynard Spiess, Sam Hay, David Leys

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)

Isobutene is a high value gaseous alkene that is widely used as fuel additive and a chemical building block. Here, the authors report an alternative pathway for isobutene bioproduction by directed evolution of prenylated FMN-dependent ferulic acid de

Externí odkaz: https://doaj.org/article/d96751d628eb4409a64c70cfafc944c0

Heterologous production, reconstitution and EPR spectroscopic analysis of prFMN dependent enzymes

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

Enzymatic control of cycloadduct conformation ensures reversible 1,3-dipolar cycloaddition in a prFMN-dependent decarboxylase

Autor: David Leys, Annica Saaret, Karl A. P. Payne, Samuel S. Bailey, Iaroslav Kosov, Stephen A. Marshall, Sam Hay, Irina Gostimskaya, Karl Fisher

Publikováno v: Nature Chemistry
Bailey, S, Payne, K, Saaret, A, Marshall, S, Gostimskaya, I, Kosov, I, Fisher, K, Hay, S & Leys, D 2019, ' Enzymatic control of cycloadduct conformation ensures reversible 1,3 dipolar cycloaddition in a prFMN dependent decarboxylase ', Nature Chemistry, vol. 11, pp. 1049-1057 . https://doi.org/10.1038/s41557-019-0324-8
Nature chemistry

The UbiD enzyme plays an important role in bacterial ubiquinone (coenzyme Q) biosynthesis. It belongs to a family of reversible decarboxylases that interconvert propenoic or aromatic acids with the corresponding alkenes or aromatic compounds using a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87c11861c3a7718bd46c89e980881861

Enzymatic C–H activation of aromatic compounds through CO2 fixation

Autor: Irina Gostimskaya, Godwin A. Aleku, Gabriel R. Titchiner, Annica Saaret, Deepankar Gahloth, David Leys, Sasha R. Derrington, David A. Parker, Ruth T. Bradshaw-Allen, Sam Hay

Publikováno v: Aleku, G, Saaret, A, Bradshaw Allen, R, Derrington, S, Titchiner, G, Gostimskaya, I, Gahloth, D, Parker, D A, Hay, S & Leys, D 2020, ' Enzymatic C-H activation of aromatic compounds through CO2 fixation ', Nature chemical biology, vol. 16, no. 11, pp. 1255-1260 . https://doi.org/10.1038/s41589-020-0603-0
Nature Chemical Biology

The direct C–H carboxylation of aromatic compounds is an attractive route to the corresponding carboxylic acids, but remains challenging under mild conditions. It has been proposed that the first step in anaerobic microbial degradation of recalcitr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef88e995d84fd23de75248751abe031f