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Literature summary for 3.1.13.2 extracted from

  • Champoux, J.J.; Schultz, S.J.
    Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription (2009), FEBS J., 276, 1506-1516.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.13.2

Application

Application Comment Organism
drug development RNase H activity associated with human immunodeficiency virus type 1 is an attractive target for an antiretroviral drug development Human immunodeficiency virus 1

Protein Variants

Protein Variants Comment Organism
additional information isolated RNase H domain of Moloney murine leukemia virus reverse transcriptase is enzymatically active, but the activity is low and exhibits a greatly relaxed substrate specificity. Primer grip residue Tyr586 in Moloney murine leukemia virus reverse transcriptase appears to be a particularly important substrate contact residue because changes at this site profoundly affect both the RNase H activity and proper substrate recognition Moloney murine leukemia virus
additional information the isolated HIV-1 RNase H domain is inactive, but the addition of various N-terminal extensions restores some RNase H activity. Changes at Trp266 and Phe61 in HIV-1 reverse transcriptase, both of which render the RNase H incapable of generating the polypurine tract (PPT) primer or removing the PPT primer once it has been extended primer grip residue Tyr501 in HIV-1 reverse transcriptase appears to be a particularly important substrate contact residue because changes at this site profoundly affect both the RNase H activity and proper substrate recognition Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
-
 Human immunodeficiency virus 1
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester 20-25 microM effectively inhibited HIV-1 replication Human immunodeficiency virus 1
additional information screening of 20000 small-molecular-weight compounds for RNase H inhibitors Human immunodeficiency virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Avian sarcoma leukosis virus
Mg2+ four highly conserved acidic amino acids (Asp443, Glu478, Asp498 and Asp549) coordinate the binding of two Mg2+ ions Human immunodeficiency virus 1
Mg2+ four highly conserved acidic amino acids (Asp524, Glu562, Asp583 and Asp653) coordinate the binding of two Mg2+ ions Moloney murine leukemia virus
Mn2+
-
 Moloney murine leukemia virus
Mn2+
-
 Avian sarcoma leukosis virus
Mn2+
-
 Human immunodeficiency virus 1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
-
 Moloney murine leukemia virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Moloney murine leukemia virus 3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages ?
-
 ?
additional information Avian sarcoma leukosis virus 3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages ?
-
 ?
additional information Human immunodeficiency virus 1 3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages ?
-
 ?
additional information Human immunodeficiency virus 1 the reverse transcriptase-associated RNase H activity introduces nicks into the RNA strand that yield low molecular weight bands in urea-containing denaturing PAGE, which are visualized by fluorescence scanning. The p51 preparation does not yield detectable low-molecular-weight bands, indicating that the reverse transcriptase preparation is not contaminated with RNase activities of bacterial origin ?
-
 ?

Organism

Organism UniProt Comment Textmining
Avian sarcoma leukosis virus
-
-
-
Human immunodeficiency virus 1 P03366
-
-
Moloney murine leukemia virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA-RNA duplex + H2O
-
 Human immunodeficiency virus 1 ?
-
 ?
DNA-RNA hybrid + H2O 3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages Avian sarcoma leukosis virus ?
-
 ?
DNA-RNA hybrid + H2O sequence preference for internal cleavage. 3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages Moloney murine leukemia virus ?
-
 ?
additional information 3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages Moloney murine leukemia virus ?
-
 ?
additional information 3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages Avian sarcoma leukosis virus ?
-
 ?
additional information 3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages Human immunodeficiency virus 1 ?
-
 ?
additional information the reverse transcriptase-associated RNase H activity introduces nicks into the RNA strand that yield low molecular weight bands in urea-containing denaturing PAGE, which are visualized by fluorescence scanning. The p51 preparation does not yield detectable low-molecular-weight bands, indicating that the reverse transcriptase preparation is not contaminated with RNase activities of bacterial origin Human immunodeficiency virus 1 ?
-
 ?

Subunits

Subunits Comment Organism
heterodimer
-
 Human immunodeficiency virus 1
heterodimer RNase H domains found in the a subunit, also contains a C-terminal region Avian sarcoma leukosis virus
monomer RNase H domain occupies the C-terminal of the protein Moloney murine leukemia virus

Synonyms

Synonyms Comment Organism
RNase H
-
 Human immunodeficiency virus 1
RNase H retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity Moloney murine leukemia virus
RNase H retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity Avian sarcoma leukosis virus
RNase H retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity Human immunodeficiency virus 1

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0026
-
 for the CRF01 A_E (93JPNH1) reverse transcriptase. pH 8.0, 37°C Human immunodeficiency virus 1 5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester
0.0038
-
 for the CRF01 A_E (93JPNH1) reverse transcriptase. pH 8.0, 37°C Human immunodeficiency virus 1 5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
0.0265
-
 for the HIV-1 clade C (93IN101) reverse transcriptase. pH 8.0, 37°C Human immunodeficiency virus 1 5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
0.0267
-
 for clade B HIV-1LAI-derived reverse transcriptase-associated RNase H activity. pH 8.0, 37°C Human immunodeficiency virus 1 5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester
0.0296
-
 for clade B HIV-1LAI-derived reverse transcriptase-associated RNase H activity. pH 8.0, 37°C Human immunodeficiency virus 1 5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
0.0322
-
 for the HIV-1 clade C (93IN101) reverse transcriptase. pH 8.0, 37°C Human immunodeficiency virus 1 5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester