| Summary: | The cloning, purification, and initial characterization of the β-carbonic anhydrase (CA, EC 4.2.1.1) from the genome of the opportunistic pathogen <i>Malassezia restricta</i> (MreCA), which a fungus involved in dandruff and seborrheic dermatitis (SD), is reported. MreCA is a protein consisting of 230 amino acid residues and shows high catalytic activity for the hydration of CO<sub>2</sub> into bicarbonate and protons, with the following kinetic parameters: k<sub>cat</sub> of 1.06 × 10<sup>6</sup> s<sup>−1</sup> and k<sub>cat</sub>/K<sub>M</sub> of 1.07 × 10<sup>8</sup> M<sup>−1</sup> s<sup>−1</sup>. It is also sensitive to inhibition by the sulfonamide acetazolamide (K<sub>I</sub> of 50.7 nM). Phylogenetically, MreCA and other CAs from various <i>Malassezia</i> species seem to be on a different branch, distinct from that of other β-CAs found in fungi, such as <i>Candida</i> spp., <i>Saccharomyces cerevisiae</i>, <i>Aspergillus fumigatus</i>, and <i>Sordaria macrospora</i>, with only <i>Cryptococcus neoformans</i> and <i>Ustilago maydis</i> enzymes clustering near MreCA. The further characterization of this enzyme and the identification of inhibitors that may interfere with its life cycle might constitute new strategies for fighting dandruff and SD.
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