A lytic enzyme isolated from P. lytica was studied with respect to its effect on pathogenic grampositive and gramnegative organisms. All the grampositive organisms were lyzed by the enzyme to this or that extent. The cells of staphylococci were the most sensitive. The gramnegative organisms were resistant. It was suggested that the lytic enzyme could be used in preparing drugs for treating certain skin diseases caused by pathogenic staphylococci.
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J Fungi (Basel)
December 2024
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia.
The basidiomycete strain LE-BIN1700 (Agaricales, ) is able to grow on agar media supplemented with individual components of lignocellulose such as lignin, cellulose, xylan, xyloglucan, arabinoxylan, starch and pectin, and also to effectively destroy and digest birch, alder and pine sawdust. produces a unique repertoire of proteins for the saccharification of the plant biomass, including predominantly oxidative enzymes such as laccases (family AA1_1 CAZymes), GMC oxidoreductases (family AA3_2 CAZymes), FAD-oligosaccharide oxidase (family AA7 CAZymes) and lytic polysaccharide monooxygenases (family LPMO X325), as well as accompanying acetyl esterases and loosenine-like expansins. Metabolomic analysis revealed that, specifically, monosaccharides and carboxylic acids were the key low molecular metabolites in the culture liquids in the experimental conditions.
View Article and Find Full Text PDFCalcif Tissue Int
January 2025
Fondazione FIRMO Onlus, Italian Foundation for the Research On Bone Diseases, Florence, Italy.
Gaucher disease is a rare lysosomal storage disorder characterized by the accumulation of glucocerebroside lipids within multiple organs due to a deficiency of the lysosomal enzyme (acid β-glucosidase). It is an inherited autosomal recessive disease. The onset of symptoms can vary depending on disease type and severity, with milder forms presenting in adulthood.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Bacterial cell wall assembly and remodeling require activities of peptidoglycan (PG) hydrolases as well as PG synthases. In particular, the activity of DD-endopeptidases, which cleave the 4-3 peptide crosslinks in PG, is essential for PG expansion in gram-negative bacteria. Maintaining optimal levels of DD-endopeptidases is critical for expanding PG without compromising its integrity.
View Article and Find Full Text PDFDalton Trans
January 2025
Department of Computational Chemistry, Lund University, Chemical Centre, P. O. Box 124, SE-221 00 Lund, Sweden.
Particulate methane monooxygenase (pMMO) is the most efficient of the two groups of enzymes that can hydroxylate methane. The enzyme is membrane bound and therefore hard to study experimentally. For that reason, there is still no consensus regarding the location and nature of the active site.
View Article and Find Full Text PDFChem Sci
January 2025
State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry College of Chemistry and Chemical Engineering, Xiamen University Xiamen 361005 China
Lytic polysaccharide monooxygenases (LPMOs) are a unique group of monocopper enzymes that exhibit remarkable ability to catalyze the oxidative cleavage of recalcitrant carbohydrate substrates, such as cellulose and chitin, by utilizing O or HO as the oxygen source. One of the key challenges in understanding the catalytic mechanism of LPMOs lies in deciphering how they activate dioxygen using diverse reductants. To shed light on this intricate process, we conducted in-depth investigations using quantum mechanical/molecular mechanical (QM/MM) metadynamics simulations, molecular dynamics (MD) simulations, and density functional theory (DFT) calculations.
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