EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.26.4 | RNase HI sequence comparisons, expression of wild-type and mutant enzymes in Escherichia coli | Thermotoga maritima |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.26.4 | additional information | the C-terminal RNase H domain loses the ability to suppress the RNase H deficiency of an Escherichia coli rnhA mutant. The substrate binding affinity of Tma-RNase HI is greatly reduced on removal of the hybrid binding domain or the mutation | Thermotoga maritima |
3.1.26.4 | W22A | site-directed mutagenesis, located in the hybrid binding domain | Thermotoga maritima |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.26.4 | 0.00039 | - |
M13 DNA/RNA hybrid | wild-type enzyme, pH 9.0, 30°C, in presence of 50 mM KCl | Thermotoga maritima |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.26.4 | KCl | activates, best at 50 mM for the full-length enzyme, and at 10 mM for the C-terminal domain | Thermotoga maritima | |
3.1.26.4 | Mg2+ | dependent on | Thermotoga maritima | |
3.1.26.4 | Mn2+ | activates, less active than Mg2+ | Thermotoga maritima | |
3.1.26.4 | additional information | Tma-RNase HI prefers Mg2+ to Mn2+ for activity, and specifically loses most of the Mg2+-dependent activity on removal of the hybrid binding domain and 87% of it by the mutation at the hybrid binding domain. Activity profiles of different metals and salt concentrations | Thermotoga maritima |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.26.4 | additional information | Thermotoga maritima | ribonuclease H is an enzyme that specifically cleaves RNA of RNA?DNA hybrids | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.26.4 | Thermotoga maritima | Q9X122 | - |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.26.4 | 0.48 | - |
substrate M13 DNA/RNA hybrid, enzyme mutant W22A, pH 9.0, 30°C, in presence of 50 mM KCl | Thermotoga maritima |
3.1.26.4 | 3.6 | - |
substrate M13 DNA/RNA hybrid, wild-type enzyme, pH 9.0, 30°C, in presence of 50 mM KCl | Thermotoga maritima |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.26.4 | D13-R4-D12-D29 hybrid + H2O | - |
Thermotoga maritima | ? | - |
? | |
3.1.26.4 | M13 DNA/RNA hybrid + H2O | - |
Thermotoga maritima | ? | - |
? | |
3.1.26.4 | additional information | ribonuclease H is an enzyme that specifically cleaves RNA of RNA?DNA hybrids | Thermotoga maritima | ? | - |
? | |
3.1.26.4 | additional information | determination of cleavage-site specificity, overview | Thermotoga maritima | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.26.4 | More | Tma-RNase HI contains a hybrid binding domain at the N-terminal region. Analysis for interaction between the C-terminal and the hybrid binding domains, overview | Thermotoga maritima |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.26.4 | RNase H | - |
Thermotoga maritima |
3.1.26.4 | RNase HI | - |
Thermotoga maritima |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.26.4 | 30 | - |
assay at | Thermotoga maritima |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.26.4 | 9 | - |
assay at | Thermotoga maritima |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.26.4 | additional information | the C-terminal RNase H domain loses the ability to suppress the RNase H deficiency of an Escherichia coli rnhA mutant, the hybrid binding domain is responsible for in vivo RNase H activity | Thermotoga maritima |