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Open AccessArticle

Phylogeny and Structure of Fatty Acid Photodecarboxylases and Glucose-Methanol-Choline Oxidoreductases

1
Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, 141700 Dolgoprudny, Russia
2
Institute of Molecular Enzyme Technology, HHU Düsseldorf, Forschungszentrum Jülich, 52428 Jülich, Germany
3
Institute of Bio- and Geosciences (IBG-1: Biotechnology), Forschungszentrum Jülich, 52428 Jülich, Germany
4
Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, 52428 Jülich, Germany
5
Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-CEA-CNRS, 38000 Grenoble, France
6
JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, 52428 Jülich, Germany
*
Authors to whom correspondence should be addressed.
Catalysts 2020, 10(9), 1072; https://doi.org/10.3390/catal10091072
Received: 21 August 2020 / Revised: 14 September 2020 / Accepted: 15 September 2020 / Published: 17 September 2020
(This article belongs to the Special Issue Biocatalysis for Green Chemistry)
Glucose-methanol-choline (GMC) oxidoreductases are a large and diverse family of flavin-binding enzymes found in all kingdoms of life. Recently, a new related family of proteins has been discovered in algae named fatty acid photodecarboxylases (FAPs). These enzymes use the energy of light to convert fatty acids to the corresponding Cn-1 alkanes or alkenes, and hold great potential for biotechnological application. In this work, we aimed at uncovering the natural diversity of FAPs and their relations with other GMC oxidoreductases. We reviewed the available GMC structures, assembled a large dataset of GMC sequences, and found that one active site amino acid, a histidine, is extremely well conserved among the GMC proteins but not among FAPs, where it is replaced with alanine. Using this criterion, we found several new potential FAP genes, both in genomic and metagenomic databases, and showed that related bacterial, archaeal and fungal genes are unlikely to be FAPs. We also identified several uncharacterized clusters of GMC-like proteins as well as subfamilies of proteins that lack the conserved histidine but are not FAPs. Finally, the analysis of the collected dataset of potential photodecarboxylase sequences revealed the key active site residues that are strictly conserved, whereas other residues in the vicinity of the flavin adenine dinucleotide (FAD) cofactor and in the fatty acid-binding pocket are more variable. The identified variants may have different FAP activity and selectivity and consequently may prove useful for new biotechnological applications, thereby fostering the transition from a fossil carbon-based economy to a bio-economy by enabling the sustainable production of hydrocarbon fuels. View Full-Text
Keywords: photocatalysis; biocatalysis; flavoprotein; oxidoreductase; fatty acid; hydrocarbon production; decarboxylase; phylogenetics; metagenomics photocatalysis; biocatalysis; flavoprotein; oxidoreductase; fatty acid; hydrocarbon production; decarboxylase; phylogenetics; metagenomics
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MDPI and ACS Style

Aleksenko, V.A.; Anand, D.; Remeeva, A.; Nazarenko, V.V.; Gordeliy, V.; Jaeger, K.-E.; Krauss, U.; Gushchin, I. Phylogeny and Structure of Fatty Acid Photodecarboxylases and Glucose-Methanol-Choline Oxidoreductases. Catalysts 2020, 10, 1072. https://doi.org/10.3390/catal10091072

AMA Style

Aleksenko VA, Anand D, Remeeva A, Nazarenko VV, Gordeliy V, Jaeger K-E, Krauss U, Gushchin I. Phylogeny and Structure of Fatty Acid Photodecarboxylases and Glucose-Methanol-Choline Oxidoreductases. Catalysts. 2020; 10(9):1072. https://doi.org/10.3390/catal10091072

Chicago/Turabian Style

Aleksenko, Vladimir A.; Anand, Deepak; Remeeva, Alina; Nazarenko, Vera V.; Gordeliy, Valentin; Jaeger, Karl-Erich; Krauss, Ulrich; Gushchin, Ivan. 2020. "Phylogeny and Structure of Fatty Acid Photodecarboxylases and Glucose-Methanol-Choline Oxidoreductases" Catalysts 10, no. 9: 1072. https://doi.org/10.3390/catal10091072

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