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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Metals Ions
Metals Ions on EC 3.1.13.2 - exoribonuclease H
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K+
Mg2+
Mn2+
Na+
LC11-RNase H1 exhibits the highest activity in the presence of 10 mM NaCl. Its activity gradually decreases as the salt concentration increases
additional information
Mg2+
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the optimum concentration of Mg2+ for activity in the presence of 3 M NaCl is 20 mM
Mg2+
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required, four RNaseH active site conserved carboxylates (the DEDD motif) coordinate two divalent cations, usually Mg2+
Mg2+
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in the presence of Mg2+ the RNase H domain clearly stabilizes the association of enzyme with primer-template
Mg2+
Asp358, Glu401 and Asp426 constitute the primary Mg2+ binding site of Ty3 RNase H domain
Mg2+
the divalent metal ion binding is important for stabilizing the structure of the isolated domain in solution
Mg2+
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1-2 ions are required for RNase H and integrase activities of the reverse transcriptase, 2 different Mg2+ ions are required for polymerase activity and are loacted in the polymerase active site of the reverse transcriptase, 3,7-dihydroxytropolone inhibitors target the Mg2+ ions, overview
Mg2+
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activates, causes conformational changes on some sites of the enzyme N-terminus near strand beta2 and beta3 and helix alphaA, residues 28-69
Mg2+
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binding of beta-thujaplicinol requires divalent metal ions
Mg2+
four highly conserved acidic amino acids (Asp443, Glu478, Asp498 and Asp549) coordinate the binding of two Mg2+ ions
Mg2+
-
optimal RNase H activity is obtained in the presence of one Mg2+ and one Mn2+
Mg2+
-
RNase H activity is slightly faster in the presence of Mg2+ than Mn2+
Mg2+
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two Mg2+ ions are bound in the catalytic center. The purified RNase H domain is stable in the presence of Mg2+ ions
Mg2+
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optimum: 2 mM for degradation of poly(A)-poly(dT), optimum: 1-2 mM for degradation of X174-DNA-RNA hybrid
Mg2+
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coordination of the magnesium ion within the catalytic core comprised of the highly conserved acidic residues D524, E562, and D583
Mg2+
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four highly conserved acidic amino acids (Asp524, Glu562, Asp583 and Asp653) coordinate the binding of two Mg2+ ions
Mn2+
folding of Halo-RNase H1 is induced by binding of Mg2+ (10 mM) to the bi/quad-aspartate site in a low-salt condition (50 mM NaCl)
Mn2+
folding of Halo-RNase H1 is induced by binding of Mn2+ (1 mM) to the bi/quad-aspartate site in a low-salt condition (50 mM NaCl)
Mn2+
-
the optimum concentration of Mn2+ for activity in the presence of 3 M NaCl is 1 mM
Mn2+
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required for the cross-linking of the modified substrate to RNase H
Mn2+
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binds to the active sites of both polymerase and RNase H
Mn2+
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optimal RNase H activity is obtained in the presence of one Mg2+ and one Mn2+
Mn2+
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optimum: 2 mM for degradation of poly(A)-poly(dT), optimum: 0.1-1.0 mM for degradation of X174DNA-RNA hybrid
Mn2+
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optimal RNase H activitiy in the presence of Mn2+ and not Mg2+
Mn2+
optimal RNase H activitiy in the presence of Mn2+ and not Mg2+
additional information
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the enzyme requires either salt or divalent metal ions for folding and is incompletely folded in the absence of both of them
additional information
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metal ions are cofactors for the catalytic activities of HIV-1 RNase H domains