Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria

Version 1 : Received: 31 October 2023 / Approved: 31 October 2023 / Online: 1 November 2023 (09:49:36 CET)

A peer-reviewed article of this Preprint also exists.

Aberuagba, A.; Joel, E.B.; Bello, A.J.; Igunnu, A.; Malomo, S.O.; Olorunniji, F.J. Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria. Int. J. Mol. Sci. 2024, 25, 1262. Aberuagba, A.; Joel, E.B.; Bello, A.J.; Igunnu, A.; Malomo, S.O.; Olorunniji, F.J. Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria. Int. J. Mol. Sci. 2024, 25, 1262.

Abstract

Protein tyrosine phosphatases (PTPs) of the polymerase and histidinol phosphatases (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 catalytic preference for Mn2+, Co2+, and Ni2+ ions. Cap8C and Wzb show an unusual thermophilic property with optimum activities over 75oC. Pre-incubation experiments show that the two enzymes are not inherently thermostable suggesting that certain catalytic step(s) in the reaction mechanism has a high activation energy. Consistent with this model, the activity-temperature profiles of the two enzymes are dependent on the divalent metal ion activating the enzyme.

Keywords

protein tyrosine phosphatases; polymerase and histidinol phosphatases; Cap8C; Wzb; metal ion activation; thermophilic enzymes

Subject

Biology and Life Sciences, Biology and Biotechnology

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.

Leave a public comment
Send a private comment to the author(s)
* All users must log in before leaving a comment
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.