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Aberuagba, A, Joel, EB, Bello, AJ, Igunnu, A, Malomo, SO and Olorunniji, FJ (2024) Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria. International Journal of Molecular Sciences, 25 (2). p. 1262. ISSN 1661-6596
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Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria.pdf - Published Version Available under License Creative Commons Attribution. Download (3MB) | Preview |
Abstract
Protein tyrosine phosphatases (PTPs) of the polymerase and histidinol phosphatase (PHP) superfamily with characteristic phosphatase activity dependent on divalent metal ions are found in many Gram-positive bacteria. Although members of this family are co-purified with metal ions, they still require the exogenous supply of metal ions for full activation. However, the specific roles these metal ions play during catalysis are yet to be well understood. Here, we report the metal ion requirement for phosphatase activities of S. aureus Cap8C and L. rhamnosus Wzb. AlphaFold-predicted structures of the two PTPs suggest that they are members of the PHP family. Like other PHP phosphatases, the two enzymes have a catalytic preference for Mn2+, Co2+ and Ni2+ ions. Cap8C and Wzb show an unusual thermophilic property with optimum activities over 75 °C. Consistent with this model, the activity–temperature profiles of the two enzymes are dependent on the divalent metal ion activating the enzyme.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Bacteria; Staphylococcus aureus; Ions; Metals; Protein Tyrosine Phosphatases; Cap8C; Wzb; metal ion activation; polymerase and histidinol phosphatases; protein tyrosine phosphatases; thermophilic enzymes; Staphylococcus aureus; Protein Tyrosine Phosphatases; Bacteria; Metals; Ions; 0399 Other Chemical Sciences; 0604 Genetics; 0699 Other Biological Sciences; Chemical Physics |
| Subjects: | R Medicine > RS Pharmacy and materia medica |
| Divisions: | Pharmacy & Biomolecular Sciences |
| Publisher: | MDPI |
| SWORD Depositor: | A Symplectic |
| Date Deposited: | 05 Feb 2024 11:08 |
| Last Modified: | 05 Feb 2024 11:15 |
| DOI or ID number: | 10.3390/ijms25021262 |
| URI: | https://researchonline.ljmu.ac.uk/id/eprint/22508 |
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