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

Authors :
Adepeju Aberuagba
Enoch B. Joel
Adebayo J. Bello
Adedoyin Igunnu
Sylvia O. Malomo
Femi J. Olorunniji
Source :
International Journal of Molecular Sciences, Vol 25, Iss 2, p 1262 (2024)
Publication Year :
2024
Publisher :
MDPI AG, 2024.

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.

Details

Language :
English
ISSN :
14220067 and 16616596
Volume :
25
Issue :
2
Database :
Directory of Open Access Journals
Journal :
International Journal of Molecular Sciences
Publication Type :
Academic Journal
Accession number :
edsdoj.5783ee5b28674c20a1ea053c648c7f5b
Document Type :
article
Full Text :
https://doi.org/10.3390/ijms25021262