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 Vinces, Tania Churasacari
A1 Souza, Anacleto Silva de
A1 Carvalho, Cecília F.
A1 Teixeira, Raphael D.
A1 Bismara, Beatriz Aparecida Passos
A1 Vicente, Elisabete J.
A1 Pereira, José O.
A1 Souza, Robson Francisco de
A1 Yonamine, Mauricio
A1 Marana, Sandro Roberto
A1 Farah, Chuck Shaker
A1 Guzzo, Cristiane R.
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.