Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase
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 n...
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Taylor & Francis Group
2022-12-01
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| Series: | Journal of Enzyme Inhibition and Medicinal Chemistry |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/14756366.2022.2131780 |
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| author | Andrea Angeli Linda J Urbański Clemente Capasso Seppo Parkkila Claudiu T. Supuran |
| author_facet | Andrea Angeli Linda J Urbański Clemente Capasso Seppo Parkkila Claudiu T. Supuran |
| author_sort | Andrea Angeli |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-e18514fffad44559bc26538e46288bea |
| institution | OA Journals |
| issn | 1475-6366 1475-6374 |
| language | English |
| publishDate | 2022-12-01 |
| publisher | Taylor & Francis Group |
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| series | Journal of Enzyme Inhibition and Medicinal Chemistry |
| spelling | doaj-art-e18514fffad44559bc26538e46288bea2025-08-20T02:36:30ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742022-12-013712786279210.1080/14756366.2022.2131780Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydraseAndrea Angeli0Linda J Urbański1Clemente Capasso2Seppo Parkkila3Claudiu T. Supuran4Dipartimento Neurofarba, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze, Sesto Fiorentino (Florence), ItalyFaculty of Medicine and Health Technology, Tampere University, Tampere, FinlandDepartment of Biology, Agriculture and Food Sciences, Institute of Biosciences and Bioresources, Napoli, ItalyFaculty of Medicine and Health Technology, Tampere University, Tampere, FinlandDipartimento Neurofarba, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze, Sesto Fiorentino (Florence), ItalyA 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.https://www.tandfonline.com/doi/10.1080/14756366.2022.2131780Staphylococcaceaecarbonic anhydraseactivatoramine/amino acidMammaliicoccus (Staphylococcus) sciuri |
| spellingShingle | Andrea Angeli Linda J Urbański Clemente Capasso Seppo Parkkila Claudiu T. Supuran Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase Journal of Enzyme Inhibition and Medicinal Chemistry Staphylococcaceae carbonic anhydrase activator amine/amino acid Mammaliicoccus (Staphylococcus) sciuri |
| title | Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase |
| title_full | Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase |
| title_fullStr | Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase |
| title_full_unstemmed | Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase |
| title_short | Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase |
| title_sort | activation studies with amino acids and amines of a β carbonic anhydrase from mammaliicoccus staphylococcus sciuri previously annotated as staphylococcus aureus saubca carbonic anhydrase |
| topic | Staphylococcaceae carbonic anhydrase activator amine/amino acid Mammaliicoccus (Staphylococcus) sciuri |
| url | https://www.tandfonline.com/doi/10.1080/14756366.2022.2131780 |
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