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Article

Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease.

International journal of molecular sciences - 1 Jan 2011

He Guang-Jun, Liu Wei-Feng, Yan Yong-Bin

Abstract excerpt

Divalent metal ions are essential for the efficient catalysis and structural stability of many nucleotidyl-transfer enzymes. Poly(A)-specific ribonuclease (PARN) belongs to the DEDD superfamily of 3'-exonucleases, and the active site of PARN contains four conserved acidic amino acid residues that coordinate two Mg(2+) ions. In this research, we studied the roles of these four acidic residues in PARN thermal...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 21686157
DOI: 10.3390/ijms12052901
PMCID: PMC3116163

Genes

PARN
DEDD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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