The cloning, purification, and initial characterization of the -carbonic anhydrase (CA, EC 4.2.1.1) from the genome of the opportunistic pathogen Malassezia restricta (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 CO2 into bicarbonate and protons, with the following kinetic parameters: k(cat) of 1.06 x 10(6) s(-1) and k(cat)/K-M of 1.07 x 10(8) M-1 s(-1). It is also sensitive to inhibition by the sulfonamide acetazolamide (K-I of 50.7 nM). Phylogenetically, MreCA and other CAs from various Malassezia species seem to be on a different branch, distinct from that of other -CAs found in fungi, such as Candida spp., Saccharomyces cerevisiae, Aspergillus fumigatus, and Sordaria macrospora, with only Cryptococcus neoformans and Ustilago maydis 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.

Cloning, Purification, and Characterization of a β-Carbonic Anhydrase from Malassezia restricta, an Opportunistic Pathogen Involved in Dandruff and Seborrheic Dermatitis / Del Prete, Sonia; Vullo, Daniela; Ghobril, Cynthia; Hitce, Julien; Clavaud, Cécile; Marat, Xavier; Capasso, Clemente; Supuran, Claudiu T. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1422-0067. - ELETTRONICO. - 20:(2019), pp. 0-0. [10.3390/ijms20102447]

Cloning, Purification, and Characterization of a β-Carbonic Anhydrase from Malassezia restricta, an Opportunistic Pathogen Involved in Dandruff and Seborrheic Dermatitis

Del Prete, Sonia;Vullo, Daniela;Supuran, Claudiu T
2019

Abstract

The cloning, purification, and initial characterization of the -carbonic anhydrase (CA, EC 4.2.1.1) from the genome of the opportunistic pathogen Malassezia restricta (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 CO2 into bicarbonate and protons, with the following kinetic parameters: k(cat) of 1.06 x 10(6) s(-1) and k(cat)/K-M of 1.07 x 10(8) M-1 s(-1). It is also sensitive to inhibition by the sulfonamide acetazolamide (K-I of 50.7 nM). Phylogenetically, MreCA and other CAs from various Malassezia species seem to be on a different branch, distinct from that of other -CAs found in fungi, such as Candida spp., Saccharomyces cerevisiae, Aspergillus fumigatus, and Sordaria macrospora, with only Cryptococcus neoformans and Ustilago maydis 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.
2019
20
0
0
Del Prete, Sonia; Vullo, Daniela; Ghobril, Cynthia; Hitce, Julien; Clavaud, Cécile; Marat, Xavier; Capasso, Clemente; Supuran, Claudiu T
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1307648
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