EC Number   |
Reaction |
Reference |
|---|
   3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
catalytic active site and substrate binding site structure and number determines the classification into classes I to III, overview |
656774 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
catalytic active site and substrate binding site structure and number determines the classification into classes I to III, overview, mechanism |
656774 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
catalytic mechanism of RNase III, overview. RNase III activates water as a nucleophile to hydrolyze target site phosphodiesters, creating 3'-hydroxyl, 5'-phosphomonoester product termini, Mg2+ serves as the ion facilitating departure of the 3'-oxygen atom, while Mg2+ binds and activates the water nucleophile. And both metal ions may coordinate to both the nucleophile and the nonbridging phosphoryl oxygen to stabilize the in-line geometry required for phosphoryl transfer reactions |
-, 750986 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
catalytic mechanism, overview. The enzyme activates water as a nucleophile to hydrolyze target site phosphodiesters, creating 3'-hydroxyl, 5'-phosphomonoester product termini |
-, 731020 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
catalytic mechanism, overview. The enzyme activates water as a nucleophile to hydrolyze target site phosphodiesters, creating 3'-hydroxyl, 5'-phosphomonoester product termini, essential irreversibility of the hydrolytic step |
731020 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
cleaves multimeric tRNA precursor at the spacer region, also involved in processing of precursor rRNA, hnRNA and early T7-mRNA. Also cleaves double-stranded DNA |
- |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
determination of specific cleavage site, Glu117 is important for phosphodiester hydrolysis |
656708 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
Glu117 is essential for phosphodiester hydrolysis but not for substrate binding, the dsRNA-binding domain is important for substrate binding but not for catalytic activity, while the catalytic domain is important for catalytic activity but not for substrate binding |
654588 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
mechanism of RNase III catalytic action, overview. Endoribonucleolytic activity of RNase III produces 2-nucleotide 3'-OH overhang at the end of dsRNA substrates |
751291 |
| 3.1.26.3 | Endonucleolytic cleavage to a 5'-phosphomonoester |
reaction mechanism, conserved Mn2+-dependent Glu117 is required, overview |
650060 |
