Biochemical analysis of catalytic and disease-associated residues in mouse Golgi-resident 3′-phosphoadenosine-5′-phosphate (PAP) phosphatase BPNT2/gPAPP

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ID: 329623
2026
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Abstract
Abstract Golgi-resident 3′-phosphoadenosine-5′-phosphate (PAP) phosphatase BPNT2/gPAPP plays an essential role in maintaining sulfation homeostasis, but its biochemical characterization has been limited by the difficulty of in vitro analyses. Here, we established a stable expression and activity assay system using a Trigger factor-fused BPNT2 construct. Using this system, we performed AlphaFold 3-guided mutational analyses. The predicted model and mutational analyses showed that several acidic residues are required for efficient PAP phosphatase activity, likely through their contribution to Mg²⁺ coordination. In addition, T177 was suggested to help maintain an active-site geometry that could accommodate a catalytic water molecule. Conservation analysis and lithium inhibition supported the idea that BPNT2 shares a conserved Mg²⁺-dependent catalytic framework with related PAP phosphatases. Disease-associated variants D175N and T181P showed substantially reduced activity, possibly due to impaired Mg2+ coordination and local structural distortion. These findings provide a biochemical framework for understanding BPNT2 function in Golgi sulfation regulation.
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openalex_W7214205223 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ryota Urushihara, Yasuhisa Maruno, Saki Maruoka, Moe Tsuruta, 遼太朗 松崎, Etsuko Nishimoto, Takamasa Teramoto, Yoshimitsu Kakuta
Journal bioscience biotechnology and biochemistry
Year 2026
DOI
10.1093/bbb/zbag144
URL
https://doi.org/10.1093/bbb/zbag144
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