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Literature summary for 5.6.2.4 extracted from
- Purification and characterization of Thermus thermophilus UvrD (2003), Extremophiles, 7, 35-41.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Thermus thermophilus HB8 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| single-stranded DNA | - |
Thermus thermophilus HB8 |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | requirement for divalent metal ions. Helicase activity is stimulated most by MgCl2 at a concentration of 1.5 mM | Thermus thermophilus HB8 | |
| Mn2+ | MnCl2 stimulates activity, though not as well as the MgCl2 | Thermus thermophilus HB8 | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Thermus thermophilus HB8 | helicase UvrD protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, and in DNA replication | ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus HB8 | O24736 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermus thermophilus HB8 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | helicase UvrD protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, and in DNA replication | Thermus thermophilus HB8 | ADP + phosphate | - |
? | |
| ATP + H2O | the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme | Thermus thermophilus HB8 | ADP + phosphate | - |
? | |
| CTP + H2O | the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme | Thermus thermophilus HB8 | CDP + phosphate | - |
? | |
| dATP + H2O | the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme | Thermus thermophilus HB8 | dADP + phosphate | - |
? | |
| dCTP + H2O | the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme | Thermus thermophilus HB8 | dCDP + phosphate | - |
? | |
| dGTP + H2O | the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme | Thermus thermophilus HB8 | dGDP + phosphate | - |
? | |
| GTP + H2O | the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme | Thermus thermophilus HB8 | GDP + phosphate | - |
? | |
| UTP + H2O | the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme | Thermus thermophilus HB8 | UDP + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| helicase UvrD | - |
Thermus thermophilus HB8 |
| Tth UvrD | - |
Thermus thermophilus HB8 |
| UvrD | - |
Thermus thermophilus HB8 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Thermus thermophilus HB8 |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | 30°C: about 65% of maximal activity, 60°C: about 75% of maximal activity | Thermus thermophilus HB8 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.9 | - |
assay at | Thermus thermophilus HB8 |
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