Publications by authors named "J Preben Morth"

The recently discovered metagenomic urethanases UMG-SP1, UMG-SP2, and UMG-SP3 have emerged as promising tools to establish a bio-based recycling approach for polyurethane (PU) waste. These enzymes are capable of hydrolyzing urethane bonds in low molecular weight dicarbamates as well as in thermoplastic PU and the amide bond in polyamide employing a Ser-Ser -Lys triad for catalysis, similar to members of the amidase signature protein superfamily. Understanding the catalytic mechanism of these urethanases is crucial for enhancing their enzymatic activity and improving PU bio-recycling processes.

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Unlabelled: This study investigates the interaction of KEIF, the intrinsically disordered N-terminal region of the magnesium transporter MgtA, with lipid bilayers mimicking cell membranes. Combining experimental techniques such as neutron reflectometry (NR), quartz-crystal microbalance with dissipation monitoring (QCM-D), synchrotron radiation circular dichroism (SRCD), and oriented circular dichroism (OCD), with molecular dynamics (MD) simulations, we characterized KEIF's adsorption behavior.

Hypothesis: KEIF undergoes conformational changes upon interacting with lipid bilayers, potentially influencing MgtA's function within the plasma membrane.

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Article Synopsis
  • GH29A α-l-fucosidases are enzymes that help break down specific sugars in glycoconjugates and can also be used to create human milk oligosaccharides (HMOs) through a process called transglycosylation.
  • Researchers used bioinformatics tools and phylogenetic clustering to identify and analyze new microbial GH29A α-l-fucosidases from an underexplored group, as well as previously known enzymes, to determine their biochemical properties and behavior under different conditions.
  • The study found that transglycosylation of certain substrates was most effective at neutral to alkaline pH levels and revealed new structural insights into how these enzymes function, particularly regarding regioselectivity in product formation.
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Global plastic production exceeded 400 million tons in 2022, urgently demanding improved waste management and recycling strategies for a circular plastic economy. While the enzymatic hydrolysis of polyethylene terephthalate (PET) has become feasible on industrial scales, efficient enzymes targeting other hydrolyzable plastic types, such as polyurethanes (PURs), are lacking. Recently, enzymes of the amidase signature (AS) family, capable of cleaving urethane bonds in a polyether-PUR analog and a linear polyester-PUR, have been identified.

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Fungal infections pose a great threat to public health and there are only four main types of antifungal drugs, which are often limited with toxicity, drug-drug interactions and antibiotic resistance. Streptomyces is an important source of antibiotics, represented by the clinical drug amphotericin B. Here we report the discovery of alligamycin A (1) as an antifungal compound from the rapamycin-producer Streptomyces iranensis through genome-mining, genetics and natural product chemistry approaches.

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