An integrated overview of bacterial carboxylesterase: Structure, function and biocatalytic applications

Johan, Ummie Umaiera Mohd.; Rahman, Raja Noor Zaliha Raja Abd; Leow, Adam Thean Chor; Ali, Mohd Shukuri Mohamad

doi:10.1016/j.colsurfb.2021.111882

Cited by 26 publications

(27 citation statements)

References 125 publications

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“…Gene peg.1365 , which encodes a putative carboxylesterase, shared a 31.5% similarity with the AA sequence of carboxylesterase involved in malathion degradation derived from Alicyclobacillus tengchongensis D-1 [ 48 ] ( Table S3 ). The carboxylesterase family is a group of esterases catalyzing the cleavage of carboxylic ester linkages [ 55 ]. Hence, we suspect that R. tibetensis FXJ9.536 also uses carboxylesterase to degrade malathion.…”

Section: Resultsmentioning

confidence: 99%

Environmental Adaptability and Organic Pollutant Degradation Capacity of a Novel Rhodococcus Species Derived from Soil in the Uninhabited Area of the Qinghai-Tibet Plateau

Huang

Ning

et al. 2022

Microorganisms

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The Qinghai-Tibet Plateau (QTP) is known for extreme natural environments and, surprisingly, has been reported to contain widespread organic pollutants. Rhodococcus can survive a variety of extreme environments and degrade many organic contaminants. Here, we isolated a Rhodococcus strain (FXJ9.536 = CGMCC 4.7853) from a soil sample collected in the QTP. Phylogenomic analysis indicated that the strain represents a novel Rhodococcus species, for which the name Rhodococcus tibetensis sp. nov. is proposed. Interestingly, R. tibetensis FXJ9.536 maintained a fast growth rate and degraded 6.2% of p-nitrophenol (4-NP) and 50.0% of malathion even at 10 °C. It could degrade 53.6% of 4-NP and 99.9% of malathion at a moderate temperature. The genome of R. tibetensis FXJ9.536 contains 4-hydroxyphenylacetate 3-monoxygenase and carboxylesterase genes, which are likely associated with the degradation of 4-NP and malathion, respectively. Further genomic analysis revealed that the strain might employ multiple strategies to adapt to the harsh QTP environment. These include synthesizing cold shock proteins, compatible solutes, secondary metabolites, and storage compounds, utilizing inorganic compounds as energy and nutrition sources, as well as degrading a range of organic pollutants. Overall, our study reveals the potential of a QTP-derived new actinobacterial species for environmental adaptation and remediation in cold regions.

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Section: Resultsmentioning

confidence: 99%

Environmental Adaptability and Organic Pollutant Degradation Capacity of a Novel Rhodococcus Species Derived from Soil in the Uninhabited Area of the Qinghai-Tibet Plateau

Huang

Ning

et al. 2022

Microorganisms

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“…The bacterial lipolytic enzymes have a catalytic triad composed of Ser, His, and Asp/Glu residues, and the catalytic Ser is located in the consensus pentapeptide motif Gly-x-Ser-x-Gly (GXSXG; Johan et al, 2021 ). The predicted catalytic triad of Est33 was formed by Ser 94 , Asp 205 , and His 233 which play the role of nucleophile, charge-relay, and proton carrier, respectively ( Figure 1 ; Supplementary Figure S1 ).…”

Section: Discussionmentioning

confidence: 99%

“…The catalytic Ser94 was located in the pentapeptide motif GVSWG, which to our knowledge is first to be described in characterized esterases. A lot of novel esterases have been identified based on their similarities of conserved pentapeptide motif GXSXG and biochemical and structural characters, phylogenetic analysis ( Johan et al, 2021 ). Substitution of any of the catalytic residues with alanine (A) caused a complete loss of enzymatic activity.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Novel Esterase Est33 From an Antarctic Bacterium: A Representative of a New Esterase Family

et al. 2022

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Studies of microorganisms from extreme environments can sometimes reveal novel proteins with unique properties. Here, we identified a novel esterase gene (Est33) from an Antarctic bacterium. The protein was expressed and purified for biochemical characterizations. Site-mutation variants including S94A, D205A, and H233A were constructed to explore the structure–function relationship of the catalytic triad of Est33, and we found mutating Ser94, Asp205, and His233 residues lead to a complete loss of enzyme activity. In addition, the catalytic Ser94 located in a conserved pentapeptide motif GVSWG. Phylogenetic analysis showed that Est33 and its closely related homologs belonged to an independent group apart from other known family members, indicating that Est33 represented a new family of esterase. The Est33 enzyme was found to be a cold-active esterase retaining 25%–100% activity from 10°C to 30°C and to have optimal catalytic activity toward p-nitrophenol acetate (30°C and pH7.5). The serine modifying reagent phenylmethylsulfonyl fluoride inhibited the activity of Est33 by 77.34%, while thiol reagents such as dithiol threitol (DTT) activated the enzyme by 3-fold. Metal chelating reagents EDTA had no effects, indicating that Est33 is not a metalloenzyme. Collectively, these results indicate that Est33 constitutes the first member of a novel esterase family XXI that has been identified.

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“…Bacterial lipolytic enzymes were divided into eight families [ 15 ]. So far, a considerable number of novel esterase has been identified, comprising 11 new families based on their biochemical and structural characters, phylogenetic analysis, and similarities of the conserved pentapeptide motif GXSXG [ 33 ]. Est19 belongs to the fourth family, namely, the HSL family, which was divided into two subfamilies, the GDSAG subfamily and the GTSAG subfamily.…”

Section: Discussionmentioning

confidence: 99%

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

et al. 2021

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Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an active serine (S) located within a highly conserved catalytic triad of Ser155, Asp253, and His282 residues. The catalytic efficiency (kcat/Km) of Est19 for the pNPC6 substrate is 148.68 s−1mM−1 at 40 °C. Replacing Glu154 juxtaposed to the critical catalytic serine with Asp (E154→D substitution) reduced the activity and catalytic efficiency of the enzyme two-fold, with little change in the substrate affinity. The wild-type enzyme retained near complete activity over a temperature range of 10–60 °C, while ~50% of its activity was retained at 0 °C. A phylogenetic analysis suggested that Est19 and its homologs may represent a new subfamily of HSL. The thermal stability and stereo-specificity suggest that the Est19 esterase may be useful for cold and chiral catalyses.

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An integrated overview of bacterial carboxylesterase: Structure, function and biocatalytic applications

Cited by 26 publications

References 125 publications

Environmental Adaptability and Organic Pollutant Degradation Capacity of a Novel Rhodococcus Species Derived from Soil in the Uninhabited Area of the Qinghai-Tibet Plateau

Environmental Adaptability and Organic Pollutant Degradation Capacity of a Novel Rhodococcus Species Derived from Soil in the Uninhabited Area of the Qinghai-Tibet Plateau

Characterization of a Novel Esterase Est33 From an Antarctic Bacterium: A Representative of a New Esterase Family

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

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