ArticleApplied and environmental microbiology2012
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.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 44 citations in OpenAlex.
- Lipases: An Overview.Methods in molecular biology (Clifton, N.J.) · 2027Review
- Screening of Marine Bacteria for Lipase Activity and Application as Whole-Cell Biocatalysts.Microorganisms · 2026Article
- Comprehensive Insights into Microbial Lipases: Unveiling Structural Dynamics, Catalytic Mechanism, and Versatile Applications.Current microbiology · 2024Review
- Whole-Genome Sequencing of a Potential Ester-Synthesizing Bacterium Isolated from Fermented Golden Pomfret and Identification of Its Lipase Encoding Genes.Foods (Basel, Switzerland) · 2022Article
- The complete genome sequence of the nitrile biocatalyst Rhodocccus rhodochrous ATCC BAA-870.BMC genomics · 2020Article
- A proposed update for the classification and description of bacterial lipolytic enzymes.PeerJ · 2019Article
- Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) fromJournal of biological research (Thessalonike, Greece) · 2018Article
- Recombinant Lipase from Gibberella zeae Exhibits Broad Substrate Specificity: A Comparative Study on Emulsified and Monomolecular Substrate.International journal of molecular sciences · 2017Article
- Screening, purification, and characterization of a novel organic solvent-tolerant esterase, Lip2, from Monascus purpureus strain M7.Extremophiles : life under extreme conditions · 2017Article
- Bacillus sp. JR3 esterase LipJ: A new mesophilic enzyme showing traces of a thermophilic past.PloS one · 2017Article
- Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7.Extremophiles : life under extreme conditions · 2016Article
- The combination of functional metagenomics and an oil-fed enrichment strategy revealed the phylogenetic diversity of lipolytic bacteria overlooked by the cultivation-based method.Microbes and environments · 2014Article
- ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions.Nucleic acids research · 2013Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
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 lipase-encoding 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.
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