3.1.13.2: exoribonuclease H
This is an abbreviated version!
For detailed information about exoribonuclease H, go to the full flat file.
Word Map on EC 3.1.13.2
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3.1.13.2
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strand
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duplex
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nucleic
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rna-dna
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single-stranded
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integrase
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r-loops
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oligodeoxynucleotides
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retrotransposons
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heteroduplexes
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transcriptases
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phosphorothioate
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retroviruses
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polypurine
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moloney
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phosphodiester
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exonuclease
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rna-dependent
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pre-mrnas
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nucleases
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oligodeoxyribonucleotides
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plus-strand
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nnrti
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template-primer
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nucleocapsids
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minus-strand
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dntp
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spliceosome
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myeloblastosis
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thumb
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endonucleolytic
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oligonucleotide-directed
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2'-o-methylated
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nevirapine
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snrnp
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oligoribonucleotide
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primer-template
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okazaki
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nonnucleoside
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rna-directed
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a-form
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efavirenz
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retroelements
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3'-exonuclease
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heteropolymeric
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phosphoramidite
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pregenomic
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hepadnavirus
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hiv-rt
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pharmacology
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medicine
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drug development
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internucleotide
- 3.1.13.2
- strand
- duplex
- nucleic
- rna-dna
-
single-stranded
-
integrase
-
r-loops
- oligodeoxynucleotides
-
retrotransposons
- heteroduplexes
- transcriptases
- phosphorothioate
- retroviruses
-
polypurine
-
moloney
-
phosphodiester
-
exonuclease
-
rna-dependent
- pre-mrnas
- nucleases
- oligodeoxyribonucleotides
-
plus-strand
-
nnrti
-
template-primer
-
nucleocapsids
-
minus-strand
- dntp
-
spliceosome
-
myeloblastosis
-
thumb
-
endonucleolytic
-
oligonucleotide-directed
-
2'-o-methylated
- nevirapine
-
snrnp
- oligoribonucleotide
-
primer-template
-
okazaki
-
nonnucleoside
-
rna-directed
-
a-form
- efavirenz
-
retroelements
- 3'-exonuclease
-
heteropolymeric
-
phosphoramidite
-
pregenomic
-
hepadnavirus
- hiv-rt
- pharmacology
- medicine
- drug development
-
internucleotide
Reaction
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid =
Synonyms
3'-to-5' RNase H, HIV RNase H, HIV-1 ribonuclease H, HIV-1 RT ribonuclease H, LC11-RNase H1, More, Prp8, retroviral reverse transcriptase RNaseH, retroviral RNase H, reverse transcriptase ribonuclease H, reverse transcriptase-associated ribonuclease H, ribonuclease H, RNase H, RNase H1, RNase HI, RNaseH, RNH, RNH1, RT RNase H, RT/RNase H, T4 RNase H, Ta11
ECTree
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Reaction
Reaction on EC 3.1.13.2 - exoribonuclease H
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
the enzyme reverse transcriptase has polymerase and RNase H activities
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
the enzyme reverse transcriptase has polymerase and RNase H activities
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.
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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.
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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.
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
two activities are present in the reverse transcriptase: polymerase and RNase H. RNase H is required for removal of the viral RNA, primer formation and removal for the synthesis of the (+) strand DNA, and specific removal of the primer tRNA used in the synthesis of the (-) strand DNA.
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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
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
the selection of 5'-end-directed cleavage sites by the retroviral RNase H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5'-end
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
the selection of 5'-end-directed cleavage sites by the retroviral RNase H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5'-end
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
RNase H catalytic cleavage mechanism for end-directed primary and secondary cleavages
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3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
RNase H domain structure and mechanism of catalysis
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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
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
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.
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