Publications by authors named "A Rompel"

Tyrosinases (TYRs) are a family of copper-containing metalloenzymes that are present in all domains of life. TYRs catalyze the reactions that start the biosynthesis of melanin, the main pigment of the animal kingdom, and are also involved in the formation of the bright colors seen on the caps of mushrooms and in the petals of flowers. TYRs catalyze the -hydroxylation and oxidation of phenols and the oxidation of catechols to the respective -quinones.

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The Preyssler-type polyoxotungstate ({PW}) belongs to the family of polyanionic metal-oxides formed by group V and VI metal ions, such as V, Mo and W, commonly known as polyoxometalates (POMs). POMs have demonstrated inhibitory effect on a significant number of ATP-binding proteins in vitro. Purinergic P2 receptors, widely expressed in eukaryotic cells, contain extracellularly oriented ATP-binding sites and play many biological roles with health implications.

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Early-life exposure to natural and synthetic chemicals can impact acute and chronic health conditions. Here, a suspect screening workflow anchored on high-resolution mass spectrometry was applied to elucidate xenobiotics in breast milk and matching stool samples collected from Nigerian mother-infant pairs (n = 11) at three time points. Potential correlations between xenobiotic exposure and the developing gut microbiome, as determined by 16S rRNA gene amplicon sequencing, were subsequently explored.

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"Mushroom tyrosinase" from the common button mushroom is the most frequently used source of tyrosinase activity, both for basic and applied research. Here, the complete tyrosinase family from Agaricus bisporus var. bisporus (abPPO1-6) was cloned from mRNA and expressed heterologously using a single protocol.

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