Cloned (Comment) | Organism |
---|---|
overexpression of RNase HII in strain Bl21 (DE3) | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics with different DNA-RNA hybrids | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activates | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant RNase HII from strain BL21(DE3) to near homogeneity by a combination of ion exchange and affinity chromatography | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Endonucleolytic cleavage to a 5'-phosphomonoester | possible mechanisms for the RNase HII-catalysed reaction consistent with the pH-dependent behaviour of the enzyme, the active sites of RNase H enzymes contain a cluster of four strictly conserved carboxylate groups, requirement for ionisation of an active site carboxylic acid for metal ion binding or correct positioning of metal ion in the enzyme-substrate complex and a role for a second active site carboxylate in general base catalysis | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA-RNA hybrid + H2O | RNase HII specifically catalyses the hydrolysis of phosphate diester linkages contained within the RNA portion of DNA/RNA hybrids, usage of 5'-fluorescent oligodeoxynucleotide substrates | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease H | - |
Escherichia coli |
RNase HII | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the logarithm of the turnover number of the enzyme increases steeply with pH until a pH-independent region is reached close to neutrality | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
the logarithm of the turnover number of the enzyme increases steeply with pH until a pH-independent region is reached close to neutrality, the pH-dependence of log 1/KM is a sigmoidal curve reaching a maximal value at higher pH, suggesting deprotonation of a residue stabilises substrate binding | Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 8 | - |
Escherichia coli |