Structural and Functional Characterization of New SsoPox Variant Points to the Dimer Interface as a Driver for the Increase in Promiscuous Paraoxonase Activity

Suzumoto, Yoko; Dim, Orly; Roviello, Giovanni N.; Worek, Franz; Sussman, Joel L.; Manco, Giuseppe

doi:10.3390/ijms21051683

Cited by 16 publications

(7 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Other bacterial enzymes capable of pesticide degradation include nitro-reductase enzymes from aerobic and anaerobic metabolism bacteria [ 10 , 28 , 33 ] and esterases from Pseudomonas fluorescens [ 25 , 34 ]. Several microorganism enzymes capable of degrading carbofuran, carbaryl, aldicarb, lindane, endosulfan, DDT, and monocrotophos also have been identified [ 11 , 20 , 22 , 26 , 28 , 35 ].…”

Section: Bioremediation Of Pesticides (Status)mentioning

confidence: 99%

The function of microbial enzymes in breaking down soil contaminated with pesticides: a review

Chia,

Hadibarata,

Kristanti

et al. 2024

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

The use of pesticides and the subsequent accumulation of residues in the soil has become a worldwide problem. Organochlorine (OC) pesticides have spread widely in the environment and caused contamination from past agricultural activities. This article reviews the bioremediation of pesticide compounds in soil using microbial enzymes, including the enzymatic degradation pathway and the recent development of enzyme-mediated bioremediation. Enzyme-mediated bioremediation is divided into phase I and phase II, where the former increases the solubility of pesticide compounds through oxidation–reduction and hydrolysis reactions, while the latter transforms toxic pollutants into less toxic or nontoxic products through conjugation reactions. The identified enzymes that can degrade OC insecticides include dehalogenases, phenol hydroxylase, and laccases. Recent developments to improve enzyme-mediated bioremediation include immobilization, encapsulation, and protein engineering, which ensure its stability, recyclability, handling and storage, and better control of the reaction.

show abstract

Section: Bioremediation Of Pesticides (Status)mentioning

confidence: 99%

The function of microbial enzymes in breaking down soil contaminated with pesticides: a review

Chia,

Hadibarata,

Kristanti

et al. 2024

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

show abstract

“…Recent reports highlighted the inherent propensity of the PLLs (Phosphotriesterase like lactonases) to serve as a QQ enzyme by improving its catalytic efficiency and altering its substrate specificity. SSPox enzyme carries a binding site for Fe 2+ and Co 2+ ( Suzumoto et al, 2020 ), whereas QsdA binds to Zn 2+ . A Co 2+ ion, after binding with SSPox interacts with the carbonyl oxygen of the lactone ring.…”

Section: Quorum Quenching Mechanismsmentioning

confidence: 99%

Molecular regulation of conditioning film formation and quorum quenching in sulfate reducing bacteria

Raya

Shreya²,

Kumar³

et al. 2022

Front. Microbiol.

View full text Add to dashboard Cite

Sensing surface topography, an upsurge of signaling biomolecules, and upholding cellular homeostasis are the rate-limiting spatio-temporal events in microbial attachment and biofilm formation. Initially, a set of highly specialized proteins, viz. conditioning protein, directs the irreversible attachment of the microbes. Later signaling molecules, viz. autoinducer, take over the cellular communication phenomenon, resulting in a mature microbial biofilm. The mandatory release of conditioning proteins and autoinducers corroborated the existence of two independent mechanisms operating sequentially for biofilm development. However, both these mechanisms are significantly affected by the availability of the cofactor, e.g., Copper (Cu). Generally, the Cu concentration beyond threshold levels is detrimental to the anaerobes except for a few species of sulfate-reducing bacteria (SRB). Remarkably SRB has developed intricate ways to resist and thrive in the presence of Cu by activating numerous genes responsible for modifying the presence of more toxic Cu(I) to Cu(II) within the periplasm, followed by their export through the outer membrane. Therefore, the determinants of Cu toxicity, sequestration, and transportation are reconnoitered for their contribution towards microbial adaptations and biofilm formation. The mechanistic details revealing Cu as a quorum quencher (QQ) are provided in addition to the three pathways involved in the dissolution of cellular communications. This review articulates the Machine Learning based data curing and data processing for designing novel anti-biofilm peptides and for an in-depth understanding of QQ mechanisms. A pioneering data set has been mined and presented on the functional properties of the QQ homolog in Oleidesulfovibrio alaskensis G20 and residues regulating the multicopper oxidase properties in SRB.

show abstract

“…Moreover, thermostable enzymes are relevant for directed evolution strategies as their robustness may buffer deleterious mutations and offer new evolutionary trajectories. − In that context, the enzyme Sso Pox isolated from the hyperthermophilic archaeon Saccharolobus solfataricus was investigated. Sso Pox is a natural lactonase with a promiscuous phosphotriesterase activity toward paraoxon (also referred to as paraoxonase) which has been considered due to its tremendous thermostability ( T m = 106 °C). − This enzyme and related variants were previously shown to decontaminate a variety of phosphotriesters, such as insecticides, chemical warfare agents, or their surrogates, and could decrease OP poisoning in animal models. − …”

Section: Introductionmentioning

confidence: 99%

Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity

Jacquet,

Billot,

Shimon

et al. 2024

JACS Au

View full text Add to dashboard Cite

Enzymatic promiscuity, the ability of enzymes to catalyze multiple, distinct chemical reactions, has been well documented and is hypothesized to be a major driver of the emergence of new enzymatic functions. Yet, the molecular mechanisms involved in the transition from one activity to another remain debated and elusive. Here, we evaluated the redesign of the active site binding cleft of lactonase SsoPox using structure-based design and combinatorial libraries. We created variants with largely improved catalytic abilities against phosphotriesters, the best ones being >1000-fold better compared to the wild-type enzyme. The observed shifts in activity specificity are large, and some variants completely lost their initial activity. The selected combinations of mutations have considerably reshaped the active site cavity via side chain changes but mostly through large rearrangements of the active site loops and changes to their conformations, as revealed by a suite of crystal structures. This suggests that a specific active site loop configuration is critical to the lactonase activity. Interestingly, analysis of high-resolution structures hints at the potential role of conformational sampling and its directionality in defining the enzyme activity profile.

show abstract

Structural and Functional Characterization of New SsoPox Variant Points to the Dimer Interface as a Driver for the Increase in Promiscuous Paraoxonase Activity

Cited by 16 publications

References 47 publications

The function of microbial enzymes in breaking down soil contaminated with pesticides: a review

The function of microbial enzymes in breaking down soil contaminated with pesticides: a review

Molecular regulation of conditioning film formation and quorum quenching in sulfate reducing bacteria

Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity

Contact Info

Product

Resources

About