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Insights into aldehyde dehydrogenase enzymes: A structural perspective

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Show simple item record Shortall, Kim Djeghader, Ahmed Magner, Edmond Soulimane, Tewfik 2021-05-25T08:55:01Z 2021-05-25T08:55:01Z 2021
dc.description peer-reviewed en_US
dc.description.abstract Aldehyde dehydrogenases engage in many cellular functions, however their dysfunction resulting in accumulation of their substrates can be cytotoxic. ALDHs are responsible for the NAD(P)-dependent oxidation of aldehydes to carboxylic acids, participating in detoxification, biosynthesis, antioxidant and regulatory functions. Severe diseases, including alcohol intolerance, cancer, cardiovascular and neurological diseases, were linked to dysfunctional ALDH enzymes, relating back to key enzyme structure. An in-depth understanding of the ALDH structure-function relationship and mechanism of action is key to the understanding of associated diseases. Principal structural features 1) cofactor binding domain, 2) active site and 3) oligomerization mechanism proved critical in maintaining ALDH normal activity. Emerging research based on the combination of structural, functional and biophysical studies of bacterial and eukaryotic ALDHs contributed to the appreciation of diversity within the superfamily. Herewith, we discuss these studies and provide our interpretation for a global understanding of ALDH structure and its purpose–including correct function and role in disease. Our analysis provides a synopsis of a common structure-function relationship to bridge the gap between the highly studied human ALDHs and lesser so prokaryotic models. en_US
dc.language.iso eng en_US
dc.publisher Frontiers Media en_US
dc.relation.ispartofseries Frontiers in Molecular Biosciences;8, 659550
dc.subject aldehyde dehydrogenase en_US
dc.subject mutations en_US
dc.subject structure-function en_US
dc.title Insights into aldehyde dehydrogenase enzymes: A structural perspective en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.identifier.doi 10.3389/fmolb.2021.659550
dc.contributor.sponsor Horizon 2020 en_US
dc.contributor.sponsor ERC
dc.relation.projectid 760827 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US

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