Any feedback?
Literature summary for 3.1.26.4 extracted from
- The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease (2011), J. Biol. Chem., 286, 10530-10539.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| simultaneous expression of GST-tagged RNASEH2B, and untagged RNASEH2A and RNASEH2C subunits from vector pGEX6P1 as polycistronic construct, in Escherichia coli strain Rosetta-2 | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant subunts in a complex containing RNASEH2B residues 2-226, full-length RNASEH2C, and RNASEH2A with catalytic site mutations D34A and D169A, X-ray diffraction structure determination and analysis at 4.1-4.4 A resolution | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A177T | naturally occuring mutation in subunit RNASEH2B, the mutation is involved in auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS. The mutation disrupts the interface between a RNASEH2B alpha-helix and the RNASEH2C kinked helix | Homo sapiens |
| D169A | active site residue mutation in subunit RNASEH2A | Homo sapiens |
| D34A | active site residue mutation in subunit RNASEH2A | Homo sapiens |
| K143I | naturally occuring mutation in subunit RNASEH2C, the mutation is involved in auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS | Homo sapiens |
| P138L | naturally occuring mutation in subunit RNASEH2C, the mutation is involved in auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS | Homo sapiens |
| P151S | naturally occuring mutation in subunit RNASEH2C, the mutation is involved in auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS | Homo sapiens |
| P76L | naturally occuring mutation in subunit RNASEH2C, the mutation is involved in auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS | Homo sapiens |
| R291H | naturally occuring mutation in subunit RNASEH2A, the mutation is involved in auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS | Homo sapiens |
| R69W | naturally occuring mutation in subunit RNASEH2C, the mutation is involved in auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | substrate hydrolysis by RNase H2 follows Michaelis-Menten kinetics | Homo sapiens | |
| 0.000027 | - |
D14R1D3:DNA18 | mutant R291H, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.000028 | - |
D14R1D3:DNA18 | wild-type enzyme, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.00003 | - |
D14R1D3:DNA18 | mutant K143I, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.000143 | - |
RNA18:DNA18 | wild-type enzyme, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.000144 | - |
RNA18:DNA18 | mutant R291H, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.000158 | - |
RNA18:DNA18 | mutant K143I, pH 8.0, temperature not specified in the publication | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | the eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and 5'RNA-DNA3'/DNA junction hybrids as substrates with similar efficiency | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O75792 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D14R1D3:DNA18 + H2O | - |
Homo sapiens | ? | - |
? | |
| additional information | the eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and 5'RNA-DNA3'/DNA junction hybrids as substrates with similar efficiency | Homo sapiens | ? | - |
? | |
| RNA18:DNA18 + H2O | - |
Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotrimer | arrangement of subunits to form an enzymatically active complex, structure of the heterotrimeric RNase H2 complex, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribonuclease H2 | - |
Homo sapiens |
| RNase H2 | - |
Homo sapiens |
| RNASEH2A | - |
Homo sapiens |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.158 | - |
D14R1D3:DNA18 | mutant R291H, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.35 | - |
D14R1D3:DNA18 | mutant K143I, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.4 | - |
D14R1D3:DNA18 | wild-type enzyme, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 0.983 | - |
RNA18:DNA18 | mutant R291H, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 2.1 | - |
RNA18:DNA18 | mutant K143I, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 3.48 | - |
RNA18:DNA18 | wild-type enzyme, pH 8.0, temperature not specified in the publication | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | mutations in each of the three RNase H2 subunits are implicated in a human auto-inflammatory disorder, Aicardi-Goutieres syndrome, AGS | Homo sapiens |
| additional information | the RNASEH2A C-terminus is a eukaryotic adaptation for binding the two accessory subunits, with residues within it required for enzymatic activity. This C-terminal extension interacts with the RNASEH2C C terminus and both are necessary to form a stable, enzymatically active heterotrimer | Homo sapiens |
| physiological function | ribonuclease H2 is the major nuclear enzyme involved in the degradation of RNA/DNA hybrids and removal of ribonucleotides misincorporated in genomic DNA | Homo sapiens |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 5 | - |
D14R1D3:DNA18 | mutant R291H, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 6.67 | - |
RNA18:DNA18 | mutant R291H, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 11.67 | - |
D14R1D3:DNA18 | mutant K143I, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 13.33 | - |
RNA18:DNA18 | mutant K143I, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 15 | - |
D14R1D3:DNA18 | wild-type enzyme, pH 8.0, temperature not specified in the publication | Homo sapiens | |
| 25 | - |
RNA18:DNA18 | wild-type enzyme, pH 8.0, temperature not specified in the publication | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
