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Literature summary for 3.1.21.10 extracted from
- Metal cofactors in the structure and activity of the fowlpox resolvase (2010), J. Mol. Biol., 399, 182-195.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D132A | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| D132C | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| D135A | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| D135C | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| D135N | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| D55A | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| D7A | site-directed mutagenesis, inactive mutant | Fowlpox virus |
| D7C | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| D7N | site-directed mutagenesis, inactive mutant, the active-site mutant resolvase holds the arms in a more planar arrangement in EDTA, Ca2+, or Mg2+ conditions | Fowlpox virus |
| E33A | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| E60A | site-directed mutagenesis, inactive mutant | Fowlpox virus |
| E60C | site-directed mutagenesis, mutant with reduced activity, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| E60N | site-directed mutagenesis, mutant with reduced activity, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| E60Q | site-directed mutagenesis, inactive mutant | Fowlpox virus |
| K102A | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
| K102R | site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme | Fowlpox virus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | comple inhibition | Fowlpox virus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | the enzyme requires Mn2+ or Mg2+ as metal cofactors | Fowlpox virus | |
| Mn2+ | preferred meta ion. The enzyme requires Mn2+ or Mg2+ as metal cofactors. Concentrations of Mn2+ above 3.3 mM inhibit cleavage | Fowlpox virus | |
| additional information | influence of metal cofactors on the activity and structure of the resolvase of fowlpox virus, overview. No activity with Ca2+, little activity with Cu2+, Fe2+, Ni2+, and Zn2+ | Fowlpox virus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Fowlpox virus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | oriented cleavage on Holliday junction 1 by FPV resolvase. Active site residues are D7, E60, K102, D132, and D135. For the wild-type complex in the presence of EDTA or Ca2+, migration is consistent with the DNA arms arranged in near-tetrahedral geometry. However, the D7N active-site mutant resolvase holds the arms in a more planar arrangement in EDTA, Ca2+, or Mg2+ conditions, implicating metal-dependent contacts at the active site in the larger architecture of the complex | Fowlpox virus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FPV resolvase | - |
Fowlpox virus |
| resolvase | - |
Fowlpox virus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Fowlpox virus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | poxvirus DNA replication generates linear concatemers containing many copies of the viral genome with inverted repeat sequences at the junctions between monomers. The inverted repeats refold to generate Holliday junctions, which are cleaved by the virus-encoded resolvase enzyme to form unit-length genomes | Fowlpox virus |
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