Reconstructing the Evolutionary History of F-dependent Dehydrogenases

Overview

Journal Sci Rep

Specialty Science

Date 2018 Dec 6

PMID 30514849

Citations 11

Authors

M Laura Mascotti

Hemant Kumar

Quoc-Thai Nguyen

Maximiliano Juri Ayub

Marco W Fraaije

Affiliations

Soon will be listed here.

Abstract

During the last decade the number of characterized F-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-dependent enzymes within the luciferase-like superfamily. By a thorough phylogenetic analysis we inferred that the F-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-dependent dehydrogenases and the F-dependent reductases. By such event, the dehydrogenases specialized in generating the reduced deazaflavin cofactor, while the reductases employ the reduced F 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-dependent glucose-6-phosphate dehydrogenases, the F-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-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-dependent dehydrogenases subfamily.

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