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• W2903173852 abstract "Abstract During the last decade the number of characterized F 420 -dependent enzymes has significantly increased. Many of these deazaflavoproteins share a TIM-barrel fold and are structurally related to FMN-dependent luciferases and monooxygenases. In this work, we traced the origin and evolutionary history of the F 420 -dependent enzymes within the luciferase-like superfamily. By a thorough phylogenetic analysis we inferred that the F 420 -dependent enzymes emerged from a FMN-dependent common ancestor. Furthermore, the data show that during evolution, the family of deazaflavoproteins split into two well-defined groups of enzymes: the F 420 -dependent dehydrogenases and the F 420 -dependent reductases. By such event, the dehydrogenases specialized in generating the reduced deazaflavin cofactor, while the reductases employ the reduced F 420 for catalysis. Particularly, we focused on investigating the dehydrogenase subfamily and demonstrated that this group diversified into three types of dehydrogenases: the already known F 420 -dependent glucose-6-phosphate dehydrogenases, the F 420 -dependent alcohol dehydrogenases, and the sugar-6-phosphate dehydrogenases that were identified in this study. By reconstructing and experimentally characterizing ancestral and extant representatives of F 420 -dependent dehydrogenases, their biochemical properties were investigated and compared. We propose an evolutionary path for the emergence and diversification of the TIM-barrel fold F 420 -dependent dehydrogenases subfamily." @default.
• W2903173852 created "2018-12-11" @default.
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• W2903173852 date "2018-12-04" @default.
• W2903173852 modified "2023-10-06" @default.
• W2903173852 title "Reconstructing the evolutionary history of F420-dependent dehydrogenases" @default.
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• W2903173852 doi "https://doi.org/10.1038/s41598-018-35590-2" @default.
• W2903173852 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6279831" @default.
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• W2903173852 hasPublicationYear "2018" @default.
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