EC Explorer

3.1.26.13

retroviral ribonuclease H

Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA [1-4]. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction [5]. 2. RNA 5′-end directed cleavage 13-19 nucleotides from the RNA end [6,7]. 3. DNA 3′-end directed cleavage 15-20 nucleotides away from the primer terminus [8-10].

RT/RNase H, retroviral reverse transcriptase RNaseH, HIV RNase H

9050-76-4

Comments: Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication. To perform this task the enzyme combines two distinct activities. The polymerase domain (EC 2.7.7.49, RNA-directed DNA polymerase) occupies the N-terminal two-thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third [13,14]. The RNase H domain of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites [15-17]

created 2009