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Literature summary extracted from
- Efficient cleavage of RNA at high temperatures by a thermostable DNA-linked ribonuclease H (2000), Protein Eng., 13, 881-886.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.26.4 | overexpression of wild-type and mutant enzymes in Escherichia coli strain HB101 | Thermus thermophilus |
| 3.1.26.4 | overexpression of wild-type and mutant enzymes in strain HB101 | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | C13A/C63A/C133A/E135C | site-directed mutagenesis, 37% activity compared to the wild-type enzyme | Escherichia coli |
| 3.1.26.4 | C13S/C63A/R135C | site-directed mutagenesis, 6.9% activity compared to the wild-type enzyme | Thermus thermophilus |
| 3.1.26.4 | C63A | site-directed mutagenesis, 94% activity compared to the wild-type enzyme | Thermus thermophilus |
| 3.1.26.4 | C63A/R135C | site-directed mutagenesis, 44% activity compared to the wild-type enzyme | Thermus thermophilus |
| 3.1.26.4 | additional information | construction of DNA-linked mutant enzyme, by cross-linking of the 15mer DNA, which is complementary to the polypurine-tract sequence of human immunodeficiency virus-1 RNA, i.e. PPT-RNA, to the thiol group of Cys13 or Cys135 of the enzyme, mutants shows 0.69% activity compared to the wild-type enzyme | Thermus thermophilus |
| 3.1.26.4 | additional information | construction of DNA-linked mutant enzyme, by cross-linking of the 15mer DNA, which is complementary to the polypurine-tract sequence of human immunodeficiency virus-1 RNA, i.e. PPT-RNA, to the thiol group of Cys135 of the enzyme, mutant shows 4.2% activity compared to the wild-type enzyme | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.4 | Escherichia coli | - |
- |
- |
| 3.1.26.4 | Thermus thermophilus | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.1.26.4 | Endonucleolytic cleavage to a 5'-phosphomonoester | active site residues are Asp10, Gu48, Asp70, His124, Asp134 | Thermus thermophilus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.4 | additional information | - |
activity of wild-type and mutant enzymes, determination by spectrophotometric assay, at different temperatures | Thermus thermophilus |
| 3.1.26.4 | additional information | - |
activity of wild-type and mutant enzymes, determination by spectrophotometric assay, at different temperatures | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.4 | PPT-RNA + H2O | single-stranded, the DNA-linked enzyme mutant shows highly reduced activity compared to the wild-type enzyme, specific cleavage of the 15mer DNA, which is complementary to the polypurine-tract sequence of human immunodeficiency virus-1 RNA | Thermus thermophilus | ? | - |
? |  |
| 3.1.26.4 | PPT-RNA + H2O | single-stranded, the DNA-linked enzyme mutant shows highly reduced activity compared to the wild-type enzyme, specific cleavage of the 15mer DNA, which is complementary to the polypurine-tract sequence of human immunodeficiency virus-1 RNA | Escherichia coli | ? | - |
? | |
| 3.1.26.4 | RNA*DNA hybrid + H2O | specific for | Thermus thermophilus | ? | - |
? | |
| 3.1.26.4 | RNA*DNA hybrid + H2O | specific for | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | More | three-dimensional structure of wild-type enzyme | Thermus thermophilus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.4 | endoribonuclease H (calf thymus) | - |
Thermus thermophilus |
| 3.1.26.4 | ERNH | - |
Escherichia coli |
| 3.1.26.4 | hybrid nuclease | - |
Thermus thermophilus |
| 3.1.26.4 | hybrid ribonuclease | - |
Thermus thermophilus |
| 3.1.26.4 | hybridase | - |
Thermus thermophilus |
| 3.1.26.4 | hybridase (ribonuclease H) | - |
Thermus thermophilus |
| 3.1.26.4 | ribonuclease H | - |
Thermus thermophilus |
| 3.1.26.4 | ribonuclease H | - |
Escherichia coli |
| 3.1.26.4 | RNA*DNA hybrid ribonucleotiohydrolase | - |
Thermus thermophilus |
| 3.1.26.4 | RNase H | - |
Thermus thermophilus |
| 3.1.26.4 | RNase H | - |
Escherichia coli |
| 3.1.26.4 | RNase HI | - |
Thermus thermophilus |
| 3.1.26.4 | RNase HI | - |
Escherichia coli |
| 3.1.26.4 | TRNH | - |
Thermus thermophilus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.4 | 30 | - |
assay at, substrate RNA*DNA hybrid | Thermus thermophilus |
| 3.1.26.4 | 30 | - |
assay at, substrate RNA*DNA hybrid | Escherichia coli |
| 3.1.26.4 | 50 | - |
DNA-C135-linked mutant, substrate PPT-RNA | Escherichia coli |
| 3.1.26.4 | 65 | - |
assay at, substrate PPT-RNA | Escherichia coli |
| 3.1.26.4 | 65 | - |
wild-type enzyme, assay at, substrate PPT-RNA, DNA-C135-linked mutant enzyme shows optimal activity with this substrate at 65°C | Thermus thermophilus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.4 | 50 | - |
DNA-linked mutant, loss of 50% activity after 15 min | Escherichia coli |
| 3.1.26.4 | 60 | - |
DNA-linked mutant, complete inactivation after 15 min | Escherichia coli |
| 3.1.26.4 | 90 | - |
DNA-linked mutant is almost fully stable after 15 min | Thermus thermophilus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.26.4 | 8 | - |
assay at | Escherichia coli |
| 3.1.26.4 | 9 | - |
assay at | Thermus thermophilus |
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