EC Number   |
Reaction |
Reference |
|---|
   3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
- |
- |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
RNase H catalytic cleavage mechanism for end-directed primary and secondary cleavages |
680758 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
RNase H domain structure and mechanism of catalysis |
681677 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
RNase H domain, part of reverse transcriptase: active site residue E478 is essential for activity |
663833 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
RNase H utilizes a two-metal ion mechanism of catalysis, the first metal ion A activates the nucleophilic water molecule and the second metal ion B, possibly in conjunction with metal ion A, stabilizes the transition state intermediate, catalytic residues are Asp443, Glu478, Asp498 and Asp549, substrate interactions, reaction mechanism and cleavage mode, overview |
682980 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
RNase H utilizes a two-metal ion mechanism of catalysis, the first metal ion A activates the nucleophilic water molecule and the second metal ion B, possibly in conjunction with metal ion A, stabilizes the transition state intermediate, substrate interactions, reaction mechanism and cleavage mode, overview |
682980 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
the enzyme reverse transcriptase has polymerase and RNase H activities |
652277, 652907 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
The enzyme reverse transcriptase has polymerase and RNase H activities, study of progressive cleavage mechanism of enzyme. Because the residual RNAs vary in length, longer RNAs require several additional cleavage events for complete removal. |
653638 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
The multifunctional enzyme possesses both RNA- and DNA-dependent DNA polymerase activity and an RNase H activity. The activity of enzyme is coordinated by a catalytic triad, E478, D443, D498, of acidic residues that bind divalent cations. |
-, 650100 |
| 3.1.13.2 | 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid |
The RNase H activity is necessary for strand transfers, which occur through a two-step mechanism. The docking, which is the first step is most efficient when the reverse transcriptase pauses in a way that makes a series of adjacent RNase H cleavages. Invasion at the site is promote at high acceptor concentration and by the presence of nucleocapsid. The locking step is the second, which is most proficient in regions of weak pausing that lack stable structure and is promoted by the chaperone properties of nucleocapsid. |
652440 |
