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

Abstract

The β-carbonic anhydrase (CA, EC 4.2.1.1) from the genome of the opportunistic pathogen Malassezia restricta (MreCA), which was recently cloned and characterised, herein has been investigated for enzymatic activation by a panel of amines and amino acids. Of the 24 compounds tested in this study, the most effective MreCA activators were L-adrenaline (K_A of 15 nM), 2-aminoethyl-piperazine/morpholine (K_As of 0.25–0.33 µM), histamine, L-4-amino-phenylalanine, D-Phe, L-/D-DOPA, and L-/D-Trp (K_As of 0.32 − 0.90 µM). The least effective activators were L-/D-Tyr, L-Asp, L-/D-Glu, and L-His, with activation constants ranging between 4.04 and 12.8 µM. As MreCA is involved in dandruff and seborrhoeic dermatitis, these results are of interest to identify modulators of the activity of enzymes involved in the metabolic processes of such fungi.

Keywords:

• Carbonic anhydrase
• activator
• β-class enzyme
• pathogenic fungi
• amine
• amino acid

Acknowledgements

WAD and CTS thank the Australian Research Council for funding. This work was financed in part by l’Oréal.

Disclosure statement

The authors have no relevant affiliations of financial involvement with any organisation or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript.