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Article

Structural determinants of the uridine-preferring specificity of RNase PL3.

Biochemistry - 16 Jul 1996

Vicentini A M, Kote-Jarai Z, Hofsteenge J

Abstract excerpt

RNase PL3 is a structurally highly conserved, pyrimidine-specific RNase, which strongly prefers to cleave at the 3'-side of uridine. Here, question of which residues are involved in determining substrate specificity is addressed. The difference in the rate of cleavage of UpA and CpA was found to result from a 375-fold larger kcat for the former substrate, whereas the values of Km were essentially the same. The...

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PMID: 8703917
DOI: 10.1021/bi960457e

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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