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Literature summary for 3.1.26.13 extracted from
- Selective inactivation of M-MuLV RT RNase H activity by site-directed PEGylation: an improved ability to synthesize long cDNA molecules (2012), New Biotechnol., 29, 285-292.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C635V | site-directed mutagenesis, the mutant shows slightly reduced reverse transcriptase and RNAse H activities compared the wild-type enzyme | Moloney murine leukemia virus |
| additional information | site-directed chemical modification of the RNase H domain by selectively PEGylating Cys635, one of the eight cysteine residues present in the reverse transcriptase, specifically inactivates its ribonucleolytic activity, PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity, overview | Moloney murine leukemia virus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | Ca2+ is non-competent analogue of the Mg2+ ion cofactor | Moloney murine leukemia virus |  |
| Mg2+ | required | 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 | Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Moloney murine leukemia virus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules | Moloney murine leukemia virus | ? | - |
? | |
| additional information | DNA binding by M-MuLV RT assay using 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex, method, overview. RNA-DNA hybrid binding and 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex by M-MuLV RT derivatives, overview | Moloney murine leukemia virus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| M-MuLV RT RNase H | - |
Moloney murine leukemia virus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Moloney murine leukemia virus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 8.5 | assay at | Moloney murine leukemia virus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity, overview | Moloney murine leukemia virus |
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