Esterase EstA6 from Pseudomonas sp. CR-611 is a novel member in the utmost conserved cluster of family VI bacterial lipolytic enzymes

Prim, Núria; Bofill, Cristina; Pastor, F. I. Javier; Dı́az, Pilar

doi:10.1016/j.biochi.2006.02.011

Cited by 25 publications

(25 citation statements)

References 26 publications

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“…1), frequently described to be inhibitors of lipase activity (3,16). On the contrary, LipR activity was usually increased by the presence of divalent cations, a fact previously reported for other lipases (3,12,16,30,36).…”

Section: Discussionmentioning

confidence: 77%

Rhodococcus sp. Strain CR-53 LipR, the First Member of a New Bacterial Lipase Family (Family X) Displaying an Unusual Y-Type Oxyanion Hole, Similar to the Candida antarctica Lipase Clan

Bassegoda

Pastor

Dı́az

2012

Appl Environ Microbiol

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Bacterial lipases constitute the most important group of biocatalysts for synthetic organic chemistry. Accordingly, there is substantial interest in developing new valuable lipases. Considering the lack of information concerning the lipases of the genus Rhodococcus and taking into account the interest raised by the enzymes produced by actinomycetes, a search for putative lipaseencoding genes from Rhodococcus sp. strain CR-53 was performed. We isolated, cloned, purified, and characterized LipR, the first lipase described from the genus Rhodococcus. LipR is a mesophilic enzyme showing preference for medium-chain-length acyl groups without showing interfacial activation. It displays good long-term stability and high tolerance for the presence of ions and chemical agents in the reaction mixture. Amino acid sequence analysis of LipR revealed that it displays four unique amino acid sequence motifs that clearly separate it from any other previously described family of bacterial lipases. Using bioinformatics tools, LipR could be related only to several uncharacterized putative lipases from different bacterial origins, all of which display the four blocks of consensus amino acid sequence motifs that contribute to define a new family of bacterial lipases, namely, family X. Therefore, LipR is the first characterized member of the new bacterial lipase family X. Further confirmation of this new family of lipases was performed after cloning Burkholderia cenocepacia putative lipase, bearing the same conserved motifs and clustering in family X. Interestingly, all lipases grouping in the new bacterial lipase family X display a Y-type oxyanion hole, a motif conserved in the Candida antarctica lipase clan but never found among bacterial lipases. This observation contributes to confirm that LipR and its homologs belong to a new family of bacterial lipases. L ipases are glycerol ester hydrolases acting on acyl glycerols to liberate free fatty acids and glycerol. They catalyze reactions involving insoluble lipid substrates at the lipid-water interface and preserve their catalytic activity in organic solvents (23), acting as powerful tools for catalyzing not only hydrolysis but also various reverse reactions such as esterifications or transesterifications in anhydrous organic solvents (16, 23). Moreover, microbial lipases catalyze reactions with high specificity, regioselectivity, and enantioselectivity, constituting the most important group of biocatalysts for synthetic organic chemistry and other biotechnological applications (4,18,34,35). Accordingly, there is substantial interest in developing new lipases for use in food, biomedical, or chemical industries (18).Despite the large number of microbial lipases identified, cloned, and characterized in the last decades (3, 11, 12, 29-31, 36, 37, 39), there are still some cultivable microbial species which are promising sources of new lipases that have not yet been explored. In this respect, many rhodococci display the ability to degrade different alkanes or show tolerance to hydrocarbo...

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Section: Discussionmentioning

confidence: 77%

Rhodococcus sp. Strain CR-53 LipR, the First Member of a New Bacterial Lipase Family (Family X) Displaying an Unusual Y-Type Oxyanion Hole, Similar to the Candida antarctica Lipase Clan

Bassegoda

Pastor

Dı́az

2012

Appl Environ Microbiol

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“…Figure 7A shows the amino acid alignment of Arabidopsis SOBER1 and At4g2295 along with the most related enzymes characterized at the biochemical level. Pseudomonas fluorescens esterase EstB (Pf EstB) belongs to a conserved cluster of family VI bacterial lipolytic enzymes (Hong et al, 1991;Prim et al, 2006) and shares 30% identity and 49% similarity with SOBER1. The human acyl protein thioesterase (Hs APT1), which shares 33% identity and 49% similarity with SOBER1, was initially characterized as a lysophospholipase (LysoPLA1) capable of hydrolyzing esters on a broad range of lysophospholipids (LysoPLs) producing free fatty acids and glycerolphosphate derivatives (Zhang and Dennis, 1988;Sugimoto et al, 1996;Wang et al, 1997aWang et al, , 2000Portilla et al, 1998).…”

Section: Sober1 Encodes An Arabidopsis Ortholog Of Acyl Proteinmentioning

confidence: 99%

A Conserved Carboxylesterase Is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE inArabidopsis

et al. 2007

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AvrBsT is a type III effector from Xanthomonas campestris pv vesicatoria that is translocated into plant cells during infection. AvrBsT is predicted to encode a Cys protease that targets intracellular host proteins. To dissect AvrBsT function and recognition in Arabidopsis thaliana, 71 ecotypes were screened to identify lines that elicit an AvrBsT-dependent hypersensitive response (HR) after Xanthomonas campestris pv campestris (Xcc) infection. The HR was observed only in the Pi-0 ecotype infected with Xcc strain 8004 expressing AvrBsT. To create a robust pathosystem to study AvrBsT immunity in Arabidopsis, the foliar pathogen Pseudomonas syringae pv tomato (Pst) strain DC3000 was engineered to translocate AvrBsT into Arabidopsis by the Pseudomonas type III secretion (T3S) system. Pi-0 leaves infected with Pst DC3000 expressing a Pst T3S signal fused to AvrBsT-HA (AvrBsT HYB -HA) elicited HR and limited pathogen growth, confirming that the HR leads to defense. Resistance in Pi-0 is caused by a recessive mutation predicted to inactivate a carboxylesterase known to hydrolyze lysophospholipids and acylated proteins in eukaryotes. Transgenic Pi-0 plants expressing the wild-type Columbia allele are susceptible to Pst DC3000 AvrBsT HYB -HA infection. Furthermore, wild-type recombinant protein cleaves synthetic p-nitrophenyl ester substrates in vitro. These data indicate that the carboxylesterase inhibits AvrBsT-triggered phenotypes in Arabidopsis. Here, we present the cloning and characterization of the SUPPRESSOR OF AVRBST-ELICITED RESISTANCE1.

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“…(Nishimura and Inouye 2000), Pseudomonas sp. (Prim et al 2006;Tserovska et al 2006), Bacillus sp. (Ding et al 2014;Metin et al 2006), Lactobacillus sp.…”

Section: Microorganisms Producing Esterasesmentioning

confidence: 99%

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

2017

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Abstract:In the pulp and paper industry, during the manufacturing process, the agglomeration of pitch particles (composed of triglycerides, fatty acids, and esters) leads to the formation of black pitch deposits in the pulp and on machinery, which impacts on the process and pulp quality. Traditional methods of pitch prevention and treatment are no longer feasible due to environmental impact and cost. Consequently, there is a need for more efficient and environmentally friendly approaches. The application of lipolytic enzymes, such as lipases and esterases, could be the sustainable solution to this problem. Therefore, an understanding of their structure, mechanism, and sources are essential. In this report, we review the microbial sources for the different groups of lipolytic enzymes, the differences between lipases and esterases, and their potential applications in the pulping industry.

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Esterase EstA6 from Pseudomonas sp. CR-611 is a novel member in the utmost conserved cluster of family VI bacterial lipolytic enzymes

Cited by 25 publications

References 26 publications

Rhodococcus sp. Strain CR-53 LipR, the First Member of a New Bacterial Lipase Family (Family X) Displaying an Unusual Y-Type Oxyanion Hole, Similar to the Candida antarctica Lipase Clan

Rhodococcus sp. Strain CR-53 LipR, the First Member of a New Bacterial Lipase Family (Family X) Displaying an Unusual Y-Type Oxyanion Hole, Similar to the Candida antarctica Lipase Clan

A Conserved Carboxylesterase Is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE inArabidopsis

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

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