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Article

Role of active site arginine residues in substrate recognition by PPM1A.

Biochemical and biophysical research communications - 3 Dec 2021

Tani Itsumi, Ito Shogo, Shirahata Yukiko, Matsuyama Yutaka, Omichinski James G, Shimohigashi Yasuyuki, Kamada Rui, Sakaguchi Kazuyasu

Abstract excerpt

Reversible protein phosphorylation is a key mechanism for regulating numerous cellular events. The metal-dependent protein phosphatases (PPM) are a family of Ser/Thr phosphatases, which uniquely recognize their substrate as a monomeric enzyme. In the case of PPM1A, it has the capacity to dephosphorylate a variety of substrates containing different sequences, but it is not yet fully understood how it recognizes...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 34637963
DOI: 10.1016/j.bbrc.2021.10.001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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