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Bioactivities of secondary metabolites of two actinomycetes Streptomyces parvulus GloL3, and Streptomyces lienomycini SK5, endophytes of two Indian medicinal herbs- Globba marantina L. and Selaginella kraussiana (Kunze) A. Braun.
Braz J Microbiol
January 2025
Microbiology and Microbial Biotechnology Laboratory, Department of Botany and Forestry, Vidyasagar University, 721102, Midnapore, West Bengal, India.
Endophytic actinomycetes are potential sources of novel pharmaceutically active metabolites, significantly advancing natural product research. In the present investigation, secondary metabolites from two endophytic actinomycetes, Streptomyces parvulus GloL3, and Streptomyces lienomycini SK5, isolated from medicinal plant taxa, Globba marantina, and Selaginella kraussiana, exhibited broad-spectrum bioactivity. Ethyl Acetate (EA) extract of SK5 showed antimicrobial activity against nine human pathogens, including Methicillin-resistant Staphylococcus aureus (MRSA), Candida tropicalis, and C.
View Article and Find Full Text PDFCharacterization of the host specificity of the SH3 cell wall binding domain of the staphylococcal phage 88 endolysin.
Arch Microbiol
January 2025
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, 43400, Malaysia.
Bacteriophages produce endolysins at the end of the lytic cycle, which are crucial for lysing the host cells and releasing virion progeny. This lytic feature allows endolysins to act as effective antimicrobial alternatives when applied exogenously. Staphylococcal endolysins typically possess a modular structure with one or two enzymatically active N-terminal domains (EADs) and a C-terminal cell wall binding domain (CBD).
View Article and Find Full Text PDFInterplay between conformational dynamics and substrate binding regulates enzymatic activity: a single-molecule FRET study.
Chem Sci
January 2025
Department of Chemical and Biological Physics, Weizmann Institute of Science Rehovot 761001 Israel
Proteins often harness extensive motions of domains and subunits to promote their function. Deciphering how these movements impact activity is key for understanding life's molecular machinery. The enzyme adenylate kinase is an intriguing example for this relationship; it ensures efficient catalysis by large-scale domain motions that lead to the enclosure of the bound substrates ATP and AMP.
View Article and Find Full Text PDFA protein corona modulates the function of mineralization-competent matrix vesicles.
JBMR Plus
February 2025
Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto 14040-901, Brazil.
Mineralizing cells release a special class of extracellular vesicles known as matrix vesicles (MV), crucial for bone mineralization. Following their release, MV anchor to the extracellular matrix (ECM), where their highly specialized enzymatic machinery facilitates the formation of seed mineral within the MV's lumen, subsequently releasing it onto the ECM. However, how MV propagate mineral onto the collagenous ECM remains unclear.
View Article and Find Full Text PDFReactive Byproducts of Plant Redox Metabolism and Protein Functions.
Acta Naturae
January 2024
St Petersburg University, St. Petersburg, 199034 Russian Federation.
Living organisms exhibit an impressive ability to expand the basic information encoded in their genome, specifically regarding the structure and function of protein. Two basic strategies are employed to increase protein diversity and functionality: alternative mRNA splicing and post-translational protein modifications (PTMs). Enzymatic regulation is responsible for the majority of the chemical reactions occurring within living cells.
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