Structure, biochemical characterization and analysis of the pleomorphism of carboxylesterase Cest-2923 from<i>Lactobacillus plantarum</i>WCFS1

Benavente, R.; Esteban-Torres, María; Acebron, I.; Rivas, Blanca de las; Múñoz, Rosario; Alvarez, Y.; Mancheño, José M.

doi:10.1111/febs.12569

Cited by 34 publications

(54 citation statements)

References 44 publications

(86 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Taken together, the E25 dimer adopts a new pattern of dimerization involving both the CAP domain and the catalytic domain, different from other reported HSL enzymes. (8,9,14). In these oligomers, both the substrate binding pocket and the active site are far away from the contact area, as shown in Fig.…”

Section: Screening and Sequence Analysis Of Lipolytic Enzyme E25mentioning

confidence: 93%

“…To date, various structures from 21 GDSAG motif subfamily enzymes have been resolved. Structural analysis reveals that microbial HSL esterases consist of two domains, a CAP domain and a catalytic domain (7)(8)(9). The CAP domain is comprised mainly of two N-terminal ␣-helices and participates in substrate binding.…”

mentioning

confidence: 99%

“…Structural analyses of these HSL oligomers reveal that multiple hydrogen bonds and hydrophobic interactions involving the central ␤-sheet in the catalytic domain contribute to their dimerization, without the involvement of the CAP domain (8,9,14). The recently resolved structure of Aes, a HSL esterase from Escherichia coli, implies that the two ␣-helices within the catalytic domain are critical for its dimerization (16).…”

mentioning

confidence: 99%

“…The recently resolved structure of Aes, a HSL esterase from Escherichia coli, implies that the two ␣-helices within the catalytic domain are critical for its dimerization (16). For reported HSLs, oligomerization is supposed not to be essential for their catalytic activities, because both the substrate binding pocket and the active site are far from the contact area (8,9,14). Dimeric EstE1 become monomeric by mutating only one residue, and the resulting mutant is still active, although with considerable reduction in thermostability (8).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Structural Basis for Dimerization and Catalysis of a Novel Esterase from the GTSAG Motif Subfamily of the Bacterial Hormone-sensitive Lipase Family

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Section: Screening and Sequence Analysis Of Lipolytic Enzyme E25mentioning

confidence: 93%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Structural Basis for Dimerization and Catalysis of a Novel Esterase from the GTSAG Motif Subfamily of the Bacterial Hormone-sensitive Lipase Family

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…However, the definite approach to assigning a molecular function to a predicted open reading frame is to isolate and biochemically characterize the corresponding protein (14). In this regard, a wide study to dissect the complex array of esterase activities in L. plantarum WCFS1 cells was designed by our group (15)(16)(17)(18)(19)(20)(21)(22)(23). From the esterases assayed, only Lp_0796 was able to hydrolyze hydroxycinnamic acids and was therefore considered a feruloyl esterase.…”

mentioning

confidence: 99%

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

Esteban-Torres

Landete

Reverón

et al. 2015

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

bLactobacillus plantarum is the lactic acid bacterial species most frequently found in the fermentation of food products of plant origin on which phenolic compounds are abundant. L. plantarum strains showed great flexibility in their ability to adapt to different environments and growth substrates. Of 28 L. plantarum strains analyzed, only cultures from 7 strains were able to hydrolyze hydroxycinnamic esters, such as methyl ferulate or methyl caffeate. As revealed by PCR, only these seven strains possessed the est_1092 gene. When the est_1092 gene was introduced into L. plantarum WCFS1 or L. lactis MG1363, their cultures acquired the ability to degrade hydroxycinnamic esters. These results support the suggestion that Est_1092 is the enzyme responsible for the degradation of hydroxycinnamic esters on the L. plantarum strains analyzed. The Est_1092 protein was recombinantly produced and biochemically characterized. Surprisingly, Est_1092 was able to hydrolyze not only hydroxycinnamic esters, since all the phenolic esters assayed were hydrolyzed. Quantitative PCR experiments revealed that the expression of est_1092 was induced in the presence of methyl ferulate, an hydroxycinnamic ester, but was inhibited on methyl gallate, an hydroxybenzoic ester. As Est_1092 is an enzyme active on a broad range of phenolic esters, simultaneously possessing feruloyl esterase and tannase activities, its presence on some L. plantarum strains provides them with additional advantages to survive and grow on plant environments. Lactobacillus plantarum is a highly versatile lactic acid bacterial species found in many different ecological niches, such as vegetables, meat, fish, and dairy products, as well as in the gastrointestinal tract (1). The genome of L. plantarum strain WCFS1 was the first to be fully sequenced, and it was, in fact, the first of any of the Lactobacillus genomes to be published (2). When the genome diversity of L. plantarum on a full genome scale was analyzed, it was revealed that L. plantarum strains are predicted to lack 9 to 20% of the genes of the L. plantarum WCFS1 reference genome, and about 50 genes appeared to be specific to strain WCFS1, as they were not found in any other strain (1). This variability confirms the flexibility of L. plantarum in its ability to adapt to different environments and growth substrates.Phenolic compounds are important constituents of food products of plant origin, as they are related to the sensory characteristics of the food and are beneficial to consumer health (3). Therefore, it is interesting to know the metabolic pathways of biosynthesis or degradation of these compounds in bacteria. L. plantarum is the lactic acid bacterium that is the most frequently found in the fermentation of food products of plant origin, being the bacterial model for the study of phenolic compound metabolism (4). Among these compounds, the metabolism of phenolic esters is greatly relevant, as they are widely spread throughout the plant kingdom (3). Esters of phenolic acids mainly belong to two distingui...

show abstract

Esterase EstK from Pseudomonas putida mt‐2: An enantioselective acetylesterase with activity for deacetylation of xylan and poly(vinylacetate)

Millar

Rahmanpour

Yuan

et al. 2017

Biotech and App Biochem

View full text Add to dashboard Cite

An extracellular esterase gene estK was identified in Pseudomonas putida mt‐2 and overexpressed at high levels in Escherichia coli. The recombinant EstK enzyme was purified and characterized kinetically against p‐nitrophenyl ester and other aryl–alkyl ester substrates and found to be selective for hydrolysis of acetyl ester substrates with high activity for p‐nitrophenyl acetate (kcat 5.5 Sec−1, KM 285 µM). Recombinant EstK was found to catalyze deacetylation of acetylated beech xylan, indicating a possible in vivo function for this enzyme, and partial deacetylation of a synthetic polymer (poly(vinylacetate)). EstK was found to catalyze enantioselective hydrolysis of racemic 1‐phenylethyl acetate, generating 1R‐phenylethanol with an enantiomeric excess of 80.4%.

show abstract

Structure, biochemical characterization and analysis of the pleomorphism of carboxylesterase Cest-2923 fromLactobacillus plantarumWCFS1

Cited by 34 publications

References 44 publications

Structural Basis for Dimerization and Catalysis of a Novel Esterase from the GTSAG Motif Subfamily of the Bacterial Hormone-sensitive Lipase Family

Structural Basis for Dimerization and Catalysis of a Novel Esterase from the GTSAG Motif Subfamily of the Bacterial Hormone-sensitive Lipase Family

A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters

Esterase EstK from Pseudomonas putida mt‐2: An enantioselective acetylesterase with activity for deacetylation of xylan and poly(vinylacetate)

Contact Info

Product

Resources

About