Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase

Andrea Angeli, Linda J. Urbański, Clemente Capasso, Seppo Parkkila, Claudiu T. Supuran

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Abstract

A β-carbonic anhydrase (CA, EC 4.2.1.1) previously annotated to be present in the genome of Staphylococcus aureus, SauBCA, has been shown to belong to another pathogenic bacterium, Mammaliicoccus (Staphylococcus) sciuri. This enzyme, MscCA, has been investigated for its activation with a series of natural and synthetic amino acid and amines, comparing the results with those obtained for the ortholog enzyme from Escherichia coli, EcoCAβ. The best MscCA activators were D-His, L- and D-DOPA, 4-(2-aminoethyl)-morpholine and L-Asn, which showed KAs of 0.12 − 0.89 µM. The least efficient activators were D-Tyr and L-Gln (KAs of 13.9 − 28.6 µM). The enzyme was also also inhibited by anions and sulphonamides, as described earlier. Endogenous CA activators may play a role in bacterial virulence and colonisation of the host which makes this research topic of great interest.

Original languageEnglish
Pages (from-to)2786-2792
Number of pages7
JournalJOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
Volume37
Issue number1
DOIs
Publication statusPublished - 2022
Publication typeA1 Journal article-refereed

Keywords

  • activator
  • amine/amino acid
  • carbonic anhydrase
  • Mammaliicoccus (Staphylococcus) sciuri
  • Staphylococcaceae

Publication forum classification

  • Publication forum level 1

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery

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