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Similar Publications

Design of a Novel Peptide with Esterolytic Activity toward PET by Mimicking the Catalytic Motif of Serine Hydrolases.

J Phys Chem B

October 2024

Materials Science and Engineering Group, Department of Materials and Production, Aalborg University, Aalborg 9220, Denmark.

Article Synopsis
  • - Serine hydrolases, while useful for recycling PET plastics, have limitations due to their 3D structure, which restricts their effective application conditions.
  • - Researchers designed a 25 amino acid thermostable peptide called HSH-25 that mimics the catalytic features of serine hydrolases and showed potential for depolymerizing PET.
  • - The study confirmed that HSH-25 exhibits enzyme-like activity in a specific pH range and was effective in degrading PET substrates, with results visualized through atomic force microscopy.
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Extracellular enzymes producing yeasts study: cost-effective production of α-amylase by a newly isolated thermophilic yeast PO27.

AIMS Microbiol

January 2024

Laboratory of Microbiological Engineering and Applications, Department of Biochemistry and Molecular and Cellular Biology, Faculty of Natural and Life Sciences, Frères Mentouri University Constantine 1, Constantine 25017, Algeria.

Enzymes are biocatalysts mainly used for their industrial potential in various applications. The present study aims to understand the enzyme production for biotechnological interest from a local yeast strain. From 100 isolates obtained from various biotopes, 78 strains were selected for their enzymatic heritage.

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Scaffold hopping via ring opening enables identification of acyclic compounds as new complement Factor D inhibitors.

Bioorg Med Chem

November 2022

Department of Discovery Chemistry, BioCryst Pharmaceuticals Inc, Discovery Center of Excellence, 2100 Riverchase Center Building 200, Suite 200, Birmingham, AL 35244, United States; Department of Discovery Bioanalytical Chemistry, BioCryst Pharmaceuticals Inc, Discovery Center of Excellence, 2100 Riverchase Center Building 200, Suite 200, Birmingham, AL 35244, United States; Department of Computational Chemistry and Structural Biology, BioCryst Pharmaceuticals Inc, Discovery Center of Excellence, 2100 Riverchase Center Building 200, Suite 200, Birmingham, AL 35244, United States. Electronic address:

The three complement pathways comprising the early phase of the complement system (the classical, lectin, and alternative pathways) act together with the innate and adaptive immune systems to protect against foreign entities and maintain tissue homeostasis. While these systems are normally under tight regulatory control, several diseases have been reported to correlate with uncontrolled activation and amplification of the alternative pathway, including paroxysmal nocturnal hemoglobinuria, atypical hemolytic uremic syndrome, C3 glomerulopathy, and age-related macular degeneration. Complement FactorD (CFD), a serine protease, is the rate-limiting enzyme for the activity of alternative pathway.

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Staphylococcal exfoliative toxins (ETs) are glutamyl endopeptidases that specifically cleave the Glu381-Gly382 bond in the ectodomains of desmoglein 1 (Dsg1) via complex action mechanisms. To date, four ETs have been identified in different strains and ETE is the most recently characterized. The unusual properties of ETs have been attributed to a unique structural feature, i.

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Salt-tolerant enzymes produced by halophilic and halotolerant microorganisms have been proposed to be used in various applications that involve high saline conditions. Considering their biotechnological significance and the current need for more efficient producers of such catalysts, the present study aimed to evaluate the extracellular proteolytic, esterolytic, cellulolytic and xylanolytic activities of some halotolerant strains, and to characterize their functional parameters. A total of 21 bacterial and fungal strains belonging to the genera , , , , , , , , and were assayed by quantitative methods.

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