Reconstructing the evolutionary history of F420-dependent dehydrogenases

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...

Full description

Saved in:
Bibliographic Details
Published in:Scientific reports 2018-12, Vol.8 (1), p.1-10, Article 17571
Main Authors: Mascotti, M. Laura, Kumar, Hemant, Nguyen, Quoc-Thai, Ayub, Maximiliano Juri, Fraaije, Marco W.
Format: Article
Language:English
Subjects:
631/114/663/2009
631/45/607/1168
82/80
82/83
Catalysis
Dehydrogenases
Enzymes
Evolution
Flavin mononucleotide
Humanities and Social Sciences
multidisciplinary
Phylogeny
Science
Science (multidisciplinary)
Sugar
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-018-35590-2