Correction to: Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi‑1, the first member of a new bacterial lipase family (XIX)

Parapouli, Maria; Foukis, Athanasios; Stergiou, Panagiota‐Yiolanda; Koukouritaki, Maria; Magklaras, Panagiotis; Gkini, Olga A.; Papamichael, Emmanuel M.; Afendra, Amalia-Sofia; Hatziloukas, Efstathios

doi:10.1186/s40709-018-0083-5

Cited by 4 publications

(2 citation statements)

References 2 publications

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“…The C 12 and C 16 substrates p NP laurate and p NP palmitate are turned over far more slowly (with k cat values less than 80 s −1 ). However, each of these substrates bind with similar affinity to the active site of Ndbn (with K m values ranging from ~0.5 mM to ~1 mM), and its k cat / K m value for p NP butyrate (~33 mM −1 s −1 ) is significantly higher than that of LipSm (~0.021 mM −1 s −1 ) [35] . Consequently, Ndbn is an effective catalyst for a broad range of substrates with extraordinary efficiency towards p NP butyrate.…”

Section: Resultsmentioning

confidence: 99%

Discovery and Mechanistic Understanding of a Lipase from Rhizorhabdus dicambivorans for Efficient Ester Aminolysis in Aromatic Amines

Wang,

Huang,

et al. 2024

ChemSusChem

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The formation of amide bonds via aminolysis of esters by lipases generates a diverse range of amide frameworks in biosynthetic chemistry. Few lipases have satisfactory activity towards bulky aromatic amines despite numerous attempts to improve the efficiency of this transformation. Here, we report the discovery of a new intracellular lipase (Ndbn) with a broad substrate scope. Ndbn turns over a range of esters and aromatic amines in the presence of water (2%; v/v), producing a high yield of multiple valuable amides. Remarkably, a higher conversion rate was observed for the synthesis of amides from substrates with aromatic amine rather than aliphatic amines. Molecular dynamics (MD) and quantum mechanical/molecular mechanical (QM/MM) studies showcase the mechanism for the preference for aromatic amines, including a more suitable orientation, shorter catalytic distances in the active site pocket and a lower reaction barrier for aromatic than for aliphatic amines. This unique lipase is thus a promising biocatalyst for the efficient synthesis of aromatic amides.

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Section: Resultsmentioning

confidence: 99%

Discovery and Mechanistic Understanding of a Lipase from Rhizorhabdus dicambivorans for Efficient Ester Aminolysis in Aromatic Amines

Wang,

Huang,

et al. 2024

ChemSusChem

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“…Arpigny et al divided lipolytic enzymes into eight families based on their differences in amino acid sequences and characteristics of conserved sequences to predict the important structural characteristics of lipolytic enzymes, secretion mechanisms and potential relationships with other enzyme families (Arpigny and Jaeger, 1999). With the development of metagenomics and other technologies, some new bacterial and fungal esterase/lipase families have been discovered based on phylogenetic criteria and other conserved sequence motifs (Zarafeta et al, 2016;Parapouli et al, 2018;Jia et al, 2019), which means that the classification of esterase hydrolases is increasingly accurate.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel thermostable alkaline lipase derived from a compost metagenomic library and its potential application in the detergent industry

Zhu

Liu

et al. 2022

Front. Microbiol.

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Using composted soil samples, a metagenomic library consisting of 36,000 clones was constructed. Then, a novel lipase, Lip54q, which belongs to the VIII family of lipolytic enzymes, was identified from the metagenomic library by functional screening. To explore the enzymatic properties of Lip54q, lip54q was heterologous expressed in Escherichia coli with a high expression level of recombinant protein up to 720 mg/L. The recombinant enzyme showed the highest activity (28,160 U/mg) against a C10 substrate at pH 9.0 and 47°C, and was stable at temperatures ≤50°C and pH 8.0–11.0. Of particular interest, the surfactants, Tween-20, Tween-80 and Tritonx-100, exhibited strong promoting effects on Lip54q activities regardless of whether low concentrations (0.1%) or high concentrations (10%) were used. Application studies of Lip54q using six commercial detergents indicated that the enzyme had strong tolerance and immersion resistance to all six detergents. The results of oil-stain removal experiments suggested that addition of the enzyme to various commercial detergents could significantly improve the abilities of these detergents to remove oil-stains. Furthermore, the results of a molecular docking analysis of Lip54q showed that both the C10 substrate and linoleic acid molecules could form hydrogen bond interactions with the catalytic amino acids, Ser-268, Glu-168, and Asp-192, in the catalytic center of the enzyme, and the hydrogen bond distances were shorter. The electrostatic attraction between the enzyme and the substrate formed by the hydrogen bond with a shorter distance is stronger, which is conducive to the formation of a more stable complex between the enzyme and the substrate, thus increasing the activity of the enzyme to such substrate. These results 1ay a good foundation for application of this enzyme in the detergent industry in the future.

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Current perspectives for microbial lipases from extremophiles and metagenomics

2021

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Correction to: Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi‑1, the first member of a new bacterial lipase family (XIX)

Cited by 4 publications

References 2 publications

Discovery and Mechanistic Understanding of a Lipase from Rhizorhabdus dicambivorans for Efficient Ester Aminolysis in Aromatic Amines

Discovery and Mechanistic Understanding of a Lipase from Rhizorhabdus dicambivorans for Efficient Ester Aminolysis in Aromatic Amines

Characterization of a novel thermostable alkaline lipase derived from a compost metagenomic library and its potential application in the detergent industry

Current perspectives for microbial lipases from extremophiles and metagenomics

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