IMIBIO-SL   20937
INSTITUTO MULTIDISCIPLINARIO DE INVESTIGACIONES BIOLOGICAS DE SAN LUIS
Unidad Ejecutora - UE
artículos
Título:
Reconstructing the evolutionary history of F420-dependent dehydrogenases
Autor/es:
NGUYEN, QT; MASCOTTI, ML; JURI AYUB, M; KUMAR, H; FRAAIJE, MW
Revista:
Scientific Reports
Editorial:
Springer Nature
Referencias:
Año: 2018
Resumen:
During the last decade the number of characterized F420-dependent enzymes has signifcantly increased. Many of these deazafavoproteins 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 F420-dependent enzymes within the luciferase-like superfamily. By a thorough phylogenetic analysis we inferred that the F420-dependent enzymes emerged from a FMN-dependent common ancestor. Furthermore, the data show that during evolution, the family of deazafavoproteins split into two well-defned groups of enzymes: the F420-dependent dehydrogenases and the F420-dependent reductases. By such event, the dehydrogenases specialized in generating the reduced deazafavin cofactor, while the reductases employ the reduced F420 for catalysis. Particularly, we focused on investigating the dehydrogenase subfamily and demonstrated that this group diversifed into three types of dehydrogenases: the already known F420-dependent glucose-6-phosphate dehydrogenases, the F420-dependent alcohol dehydrogenases, and the sugar-6-phosphate dehydrogenases that were identifed in this study. By reconstructing and experimentally characterizing ancestral and extant representatives of F420-dependent dehydrogenases, their biochemical properties were investigated and compared. We propose an evolutionary path for the emergence and diversifcation of the TIM-barrel fold F -dependent dehydrogenases subfamily.