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Literature summary for 4.2.99.B1 extracted from
- Rev1 is a base excision repair enzyme with 5'-deoxyribose phosphate lyase activity (2016), Nucleic Acids Res., 44, 10824-10833 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Rev1, recombinant expression of His-tagged full-length enzyme in in Escherichia coli | Mus musculus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic analysis of dRP lyase activity of the C-terminal domain of Rev1 using a 34-bp duplex DNA substrate. The substrate contained an 18mer DNA strand with 6-FAM at the 3'- end and 5'-RP flap at the margin of a single-nucleotide gap | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged full-length enzyme Rev1 from in Escherichia coli, tag removal | Mus musculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | dRP lyase activity of the C-terminal domain of Rev1. Preparation of the 3'-end labeled dRP lyase substrate: 32P-labeled duplex DNA is pretreated with UDG and APE1 to prepare the single-nucleotide gapped substrates that contain 5'-dRP (5'-deoxyribose phosphate) flap and a 3'-OH at the margins, the S-S bond is included in the substrate molecule, overview. In vitro base excision repair (BER) activity. For kinetic analysis, a 34-bp duplex DNA substrate is prepared by annealing three DNA strands. The substrate contains an 18mer DNA strand with 6-FAM at the 3'-end and 5'-RP flap at the margin of a single-nucleotide gap | Mus musculus | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | Rev1 domain mapping of the C-terminal domain by limited proteolysis | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5'-deoxyribose phosphate lyase | - |
Mus musculus |
| dRP lyase | - |
Mus musculus |
| Rev1 | - |
Mus musculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mus musculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme Rev1 is a member of the Y-family of DNA polymerases. Characterization of Rev1 domains in relation to BER activities | Mus musculus |
| physiological function | Rev1 is a base excision repair enzyme with 5'-deoxyribose phosphate lyase activity, dRP lyase activity of the C-terminal domain of Rev1. Rev1 also has deoxycytidyl transferase activity (EC 2.7.7.-) that incorporates dCMP into DNA and its ability to function as a scaffold factor for other Y-family polymerases in translesion bypass events. Rev1 also is involved in mutagenic processes during somatic hypermutation of immunoglobulin genes. Mouse fibroblast cells lacking pol beta have a DNA repair deficiency and a phenotype of elevated methyl methanesulfonate (MMS)-induced mutations. Enzyme Rev1 is strictly required for the elevated MMS-induced mutagenesis phenotype as observed in the pol beta null background, mechanisms of the Rev1-mediated MMS-induced mutagenesis, overview | Mus musculus |
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Release 2023.1 (January 2023)
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