RT Journal Article
SR Electronic
T1 Molecular and functional basis of a novel Amazonian Dark Earth Esterase 1 (Ade1) with hysteresis behavior and quorum-quenching activity
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.12.16.421545
DO 10.1101/2020.12.16.421545
A1 Tania Churasacari Vinces
A1 Anacleto Silva de Souza
A1 Cecília F. Carvalho
A1 Raphael D. Teixeira
A1 Beatriz Aparecida Passos Bismara
A1 Elisabete J. Vicente
A1 José O. Pereira
A1 Robson Francisco de Souza
A1 Mauricio Yonamine
A1 Sandro Roberto Marana
A1 Chuck Shaker Farah
A1 Cristiane R. Guzzo
YR 2020
UL http://biorxiv.org/content/early/2020/12/16/2020.12.16.421545.abstract
AB Amazon Dark Earth (ADE) soil is rich in organic compounds and its fertility has been associated with a high diversity of microorganisms. Herein, we investigate the biochemical and functional features of a novel esterase, Ade1, obtained from a metagenomic library of Amazonian Dark Earth soils of the Amazonian Rainforest, in Brazil. The esterases cleave ester bonds to form a carboxylic and an alcohol group. Esterases and lipases are enzymes found in almost all living organisms, demonstrating their biological relevance. We reported that Ade1 belongs to an α/β-hydrolase superfamily. We suggest that Ade1 is a moonlighting enzyme with hysteresis behavior and quorum-quenching activity, which may play a key role in the metabolism of a Gram-negative proteobacteria. In addition, molecular dynamics simulations reveal that the hysteresis behavior is directly associated with structural properties of the cap domain. Our findings reveal details of the molecular basis, catalytic and structural mechanisms of a novel α/β-hydrolase, which may be applied to other esterases of biotechnological, food, and/or pharmaceutical interest.Competing Interest StatementThe authors have declared no competing interest.