Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase. (31st December 2022)

• Record Type: Journal Article
• Authors: Angeli, Andrea; Urbański, Linda J; Capasso, Clemente; Parkkila, Seppo; Supuran, Claudiu T.
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 37:Number 1(2022)
• Page Start: 2786
• Page End: 2792
• Publication Date: 2022-12-31
• Subjects: Staphylococcaceae -- carbonic anhydrase -- activator -- amine/amino acid -- Mammaliicoccus (Staphylococcus) sciuri; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.1080/14756366.2022.2131780
• Languages: English
• ISSNs: 1475-6366

Abstract

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 KA s of 0.12 − 0.89 µM. The least efficient activators were D-Tyr and L-Gln (KA s 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.