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

@article{delPrete2019CloningPA,
  title={Cloning, Purification, and Characterization of a $\beta$-Carbonic Anhydrase from Malassezia restricta, an Opportunistic Pathogen Involved in Dandruff and Seborrheic Dermatitis},
  author={Sonia del Prete and Daniela Vullo and Cynthia Ghobril and Julien Hitce and C{\'e}cile Clavaud and Xavier Marat and Clemente Capasso and Claudiu Trandafir Supuran},
  journal={International Journal of Molecular Sciences},
  year={2019},
  volume={20}
}
The cloning, purification, and initial characterization of the β-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: kcat of 1.06 × 106 s−1 and kcat/KM of 1.07 × 108 M−1 s−1… 
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Sulfonamide Inhibition Profile of the β-Carbonic Anhydrase from Malassezia restricta, An Opportunistic Pathogen Triggering Scalp Conditions

The sulfonamide inhibition profile of the homologous β-CA (MreCA) identified in the genome of Malassezia restricta, an opportunistic pathogen triggering dandruff and seborrheic dermatitis, was investigated and might be useful for designing CA inhibitor scaffolds that may selectively inhibit the d andruff-producing fungi.

Anion Inhibition Profile of the β-Carbonic Anhydrase from the Opportunist Pathogenic Fungus Malassezia restricta Involved in Dandruff and Seborrheic Dermatitis

The anion inhibition profile is essential for better understanding the inhibition/catalytic mechanisms of these enzymes and for designing novel types of inhibitors, which may have clinical applications for the management of dandruff and seborrheic dermatitis.

Escherichia coli γ-carbonic anhydrase: characterisation and effects of simple aromatic/heterocyclic sulphonamide inhibitors

The hypothesis that the synthesis of new drugs capable of interfering selectively with the bacterial CA activity, avoiding the inhibition of the human α -CAs, is achievable and may lead to novel antibacterials is reinforced.

Activation studies of the β-carbonic anhydrases from Malassezia restricta with amines and amino acids

The β-carbonic anhydrase from the genome of the opportunistic pathogen Malassezia restricta, which was recently cloned and characterised, has been investigated for enzymatic activation by a panel of amines and amino acids to identify modulators of the activity of enzymes involved in the metabolic processes of such fungi.

Inhibitory Effects of Sulfonamide Derivatives on the β-Carbonic Anhydrase (MpaCA) from Malassezia pachydermatis, a Commensal, Pathogenic Fungus Present in Domestic Animals

Novel candidates that can kill this harmful fungus by inhibiting their CA are described, and thus lead to effective anti-dandruff and anti-seborrheic dermatitis agents.

Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii

Burkholderia territorii, a Gram-negative bacterium, encodes for the ι-class carbonic anhydrase, which is recently characterised, is proved to be a zinc(II)- and not manganese(II-containing enzyme, as reported for diatomι-CAs.

Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii

For the first time, the recombinant bacterial ι-CA (acronym BteCAι) identified in the genome of Burkholderia territorii is cloned, expressed, and purified and showed that the enzyme is formed by two equivalent monomers having a structure similar to a butterfly.

Anion Inhibition Studies of the Beta-Carbonic Anhydrase from Escherichia coli

The kinetic properties and the anion inhibition profiles of recombinant CynT2 allowed for a detailed understanding of the interaction of inhibitors with the amino acid residues surrounding the catalytic pocket of the enzyme and may be used as leads for the design of more efficient and specific inhibitors.

The Effect of Substituted Benzene-Sulfonamides and Clinically Licensed Drugs on the Catalytic Activity of CynT2, a Carbonic Anhydrase Crucial for Escherichia coli Life Cycle

The sulfonamide inhibition profile of the recombinant β-CA (CynT2) identified in the genome of the Gram-negative bacterium Escherichia coli is investigated, showing that CynT2 was strongly inhibited by some substituted benzene-sulfonamides and the clinically used inhibitor sulpiride.

Characterization of Oral Microbiota in Cats: Novel Insights on the Potential Role of Fungi in Feline Chronic Gingivostomatitis

The data suggest that fungi might play a role in the etiology and pathogenesis of FCGS, and that oral health should not simply be regarded as the absence of microbial infections, but may be viewed as the biological interactions between bacterial and fungal populations that coexist to preserve a complex equilibrium in the microenvironment of the mouth.

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