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...
Topics
- Animals
- Binding Sites
- Cytidine
- Dinucleoside Phosphates
- Endoribonucleases
- Escherichia coli
- Hydrogen Bonding
- Kinetics
- Liver
- Models, Molecular
- Molecular Structure
- Mutagenesis, Site-Directed
- Mutation
- Poly C
- Poly U
- Recombinant Proteins
- Substrate Specificity
- Swine
