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In silico and in vitro studies of the reduction of unsaturated alpha,beta bonds of trans-2-hexenedioic acid and 6-amino-trans-2-hexenoic acid - Important steps towards biobased production of adipic acid

Artikel i vetenskaplig tidskrift
Författare E. Karlsson
J. H. Shin
G. Westman
Leif A Eriksson
L. Olsson
V. Mapell
Publicerad i Plos One
Volym 13
Nummer/häfte 2
ISSN 1932-6203
Publiceringsår 2018
Publicerad vid Institutionen för kemi och molekylärbiologi
Språk en
Länkar https://doi.org/10.1371/journal.pon...
Ämnesord old yellow enzyme, high-level conversion, escherichia-coli, l-lysine, corynebacterium-glutamicum, ligand-binding, pathway, biosynthesis, aminotransferase, flavoproteins, Science & Technology - Other Topics
Ämneskategorier Biokemi och molekylärbiologi


The biobased production of adipic acid, a precursor in the production of nylon, is of great interest in order to replace the current petrochemical production route. Glucose-rich lignocellulosic raw materials have high potential to replace the petrochemical raw material. A number of metabolic pathways have been proposed for the microbial conversion of glucose to adipic acid, but achieved yields and titers remain to be improved before industrial applications are feasible. One proposed pathway starts with lysine, an essential metabolite industrially produced from glucose by microorganisms. However, the drawback of this pathway is that several reactions are involved where there is no known efficient enzyme. By changing the order of the enzymatic reactions, we were able to identify an alternative pathway with one unknown enzyme less compared to the original pathway. One of the reactions lacking known enzymes is the reduction of the unsaturated a,6 bond of 6-amino-trans-2-hexenoic acid and trans-2-hexenedioic acid. To identify the necessary enzymes, we selected N-ethylmaleimide reductase from Escherichia coli and Old Yellow Enzyme 1 from Saccharomyces pastorianus. Despite successful in silico docking studies, where both target substrates could fit in the enzyme pockets, and hydrogen bonds with catalytic residues of both enzymes were predicted, no in vitro activity was observed. We hypothesize that the lack of activity is due to a difference in electron withdrawing potential between the naturally reduced aldehyde and the carboxylate groups of our target substrates. Suggestions for protein engineering to induce the reactions are discussed, as well as the advantages and disadvantages of the two metabolic pathways from lysine. We have highlighted bottlenecks associated with the lysine pathways, and proposed ways of addressing them.

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