Any feedback?
Literature summary for 5.6.2.4 extracted from
- Biochemical characterization of the DNA substrate specificity of Werner syndrome helicase (2002), J. Biol. Chem., 277, 23236-23245.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| streptavidin | the enzyme is completely blocked by streptavidin bound to the 3'-ssDNA tail 6 nucleotides upstream of the single-stranded/double-stranded DNA junction. The enzyme efficiently unwinds the forked duplex with streptavidin bound just upstream of the junction, suggesting that the enzyme recognizes elements of the fork structure to initiate unwinding | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Homo sapiens | the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide, suggesting a role of the enzyme in Okazaki fragment processing. The ability of the enzyme to target DNA replication/repair intermediates may be relevant to its role in genome stability maintenance | ADP + phosphate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q14191 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide, suggesting a role of the enzyme in Okazaki fragment processing. The ability of the enzyme to target DNA replication/repair intermediates may be relevant to its role in genome stability maintenance | Homo sapiens | ADP + phosphate | - |
? | |
| ATP + H2O | the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide | Homo sapiens | ADP + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Werner Syndrome helicase | - |
Homo sapiens |
| WRN | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
