3.1.26.13: retroviral ribonuclease H
This is an abbreviated version!
For detailed information about retroviral ribonuclease H, go to the full flat file.
Word Map on EC 3.1.26.13
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3.1.26.13
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integrase
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hiv-rt
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rna-dna
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template-primer
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moloney
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polypurine
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transcriptases
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minus-strand
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3'-azido-3'-deoxythymidine
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nnrti
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primer-template
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nonnucleoside
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drug development
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medicine
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analysis
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pharmacology
- 3.1.26.13
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integrase
- hiv-rt
- rna-dna
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template-primer
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moloney
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polypurine
- transcriptases
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minus-strand
- 3'-azido-3'-deoxythymidine
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nnrti
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primer-template
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nonnucleoside
- drug development
- medicine
- analysis
- pharmacology
Reaction
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. 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. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. =
Synonyms
HIV reverse transcriptase ribonuclease H, HIV reverse transcriptase-associated RNase H, HIV RNase H, HIV RT RNaseH, HIV RT-associated RNase H, HIV-1 reverse transcriptase, HIV-1 reverse transcriptase ribonuclease H, HIV-1 reverse transcriptase RNase H, HIV-1 RH, HIV-1 ribonuclease H, HIV-1 ribonuclease H domain, HIV-1 RNase H, HIV-1 RT-associated RNase H, human immunodeficiency virus reverse transcriptase, human immunodeficiency virus reverse transcriptase-associated ribonuclease H, human immunodeficiency virus reverse transcriptase-associated RNase H, human immunodeficiency virus RT-associated RNase H, M-MuLV RT RNase H, reverse transcriptase, reverse transcriptase-associated ribonuclease H, reverse transcriptase-associated RNase H, reverse-transcriptase-associated ribonuclease H, ribonuclease H, ribonuclease H domain in HIV-1 reverse transcriptase, RNase H, RNase H activity of HIV-1 reverse transcriptase, RNase H domain of HIV-1 reverse transcriptase, RNase H of HIV-1 subtype C, RNaseH, RNH, RNHHIV, RT RNase H, RT-RNase H
ECTree
3.1.26.13 retroviral ribonuclease HAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.1.26.13 - retroviral ribonuclease H
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
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5'end-directed RNase H of reverse transcriptase
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additional information
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HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities
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additional information
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RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
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additional information
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conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview
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additional information
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a DNA/RNA hybrid can simultaneously engage both active sites. Of the tested interconverting reverse transcriptase-DNA/RNA species, 43% are active for both sites simultaneously, 27% show only polymerase activity, and the remaining 30% are nonproductive. A string of at least 4-6 nucleotides downstream of the cleaving site is required for efficient RNA cleavage. During processive nucleotide incorporation, sequential rounds of RNA cleavage occur each time after about 6 nucleotides are incorporated, during processive primer extension, diphosphate release is rate-limiting. Although polymerization is efficient and processive, RNase H is inefficient and periodic. This combination allows the two catalytic centers of HIVRT to work simultaneously at similar speeds without being tightly coupled
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additional information
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HIV RNase H cleaves viral RNA at multiple stages of reverse transcription with at least three distinct modes: random internal cleavages, DNA 3' end-directed and polymerase dependent cleavages, and RNA 5' end-directed cleavages. A biochemical assay uses the HTS-1 RNA/DNA substrate to specifically probe random internal cleavage, which is believed to be the dominant mode of RNA cutting
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additional information
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RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
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additional information
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Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules
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additional information
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Moloney murine leukemia virus reverse transcriptase, MMLV RT, shows DNA polymerization activity and RNase H activity. Stabilization of the reverse transcriptase activity by eliminating the RNase H activity, overview
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additional information
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retroviral reverse transcriptase also possesses a ribonuclease H activity, an enzyme which cleaves the RNA strand of RNA/DNA hetroduplex
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