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

被引：1

作者：

Aberuagba, Adepeju ^{[1
]}

Joel, Enoch B. ^{[1
,2
]}

Bello, Adebayo J. ^{[1
]}

Igunnu, Adedoyin ^{[3
]}

Malomo, Sylvia O. ^{[3
]}

Olorunniji, Femi J. ^{[1
]}

机构：

[1] Liverpool John Moores Univ, Sch Pharm & Biomol Sci, Byrom St, Liverpool L3 3AF, England

[2] Univ Jos, Fac Basic Med Sci, Dept Biochem, Jos 930003, Nigeria

[3] Univ Ilorin, Fac Life Sci, Dept Biochem, Ilorin 234031, Nigeria

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2024年 / 25卷 / 02期

关键词：

protein tyrosine phosphatases; polymerase and histidinol phosphatases; Cap8C; Wzb; metal ion activation; thermophilic enzymes; STREPTOCOCCUS-PNEUMONIAE; CAPSULE BIOSYNTHESIS; CRYSTAL-STRUCTURES; ESCHERICHIA-COLI; CPSB; POLYMERASE; PURIFICATION; ENZYMES; FAMILY;

D O I：

10.3390/ijms25021262

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 degrees C. Consistent with this model, the activity-temperature profiles of the two enzymes are dependent on the divalent metal ion activating the enzyme.

引用

页数：17

共 49 条

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