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Article

Mechanism of the phosphatase component of Clostridium thermocellum polynucleotide kinase-phosphatase.

RNA (New York, N.Y.) - 1 Jan 2006

Keppetipola Niroshika, Shuman Stewart

Abstract excerpt

Polynucleotide kinase-phosphatase (Pnkp) from Clostridium thermocellum catalyzes ATP-dependent phosphorylation of 5'-OH termini of DNA or RNA polynucleotides and Ni(2+)/Mn(2+)-dependent dephosphorylation of 2',3' cyclic phosphate, 2'-phosphate, and 3'-phosphate ribonucleotides. CthPnkp is an 870-amino-acid polypeptide composed of three domains: an N-terminal module similar to bacteriophage T4 polynucleotide...

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Identifiers

PMID: 16301605
DOI: 10.1261/rna.2196406
PMCID: PMC1370887

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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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