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Literature summary extracted from

  • Spies, M.; Kil, Y.; Masui, R.; Kato, R.; Kujo, C.; Ohshima, T.; Kuramitsu, S.; Lanzov, V.
    The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA-dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75°C (2000), Eur. J. Biochem., 267, 1125-1137.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.4.B7 ssDNA at 75°C, all DNAs tested stimulated ATPase activity of the RadA. The ssDNA-dependent ATPase activity of displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature Pyrobaculum islandicum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.4.B7
-
 Pyrobaculum islandicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.4.B7 49
-
 ATP pH 7.7, 80°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 53
-
 ATP pH 7.7, 82°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 54
-
 ATP pH 7.7, 75°C, 0.02 mM poly(dC) Pyrobaculum islandicum
3.6.4.B7 54
-
 ATP pH 7.7, 85°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 54
-
 ATP pH 7.7, °C, 0.02 mM M13mp18ssDNA Pyrobaculum islandicum
3.6.4.B7 57
-
 ATP pH 7.7, °C, 0.02 mM M13mp19dsDNA Pyrobaculum islandicum
3.6.4.B7 65
-
 ATP pH 7.7, 75°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 96
-
 ATP pH 7.7, 70°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 121
-
 ATP pH 7.7, 90°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 122
-
 ATP pH 7.7, 75°C, 0.02 mM poly(dA) Pyrobaculum islandicum
3.6.4.B7 123
-
 ATP pH 7.7, 65°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 409
-
 ATP pH 7.7, 55°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 484
-
 ATP pH 7.7, 75°C, 0.02 mM DNA Pyrobaculum islandicum
3.6.4.B7 531
-
 ATP pH 7.7, 37°C, 0.02 mM poly(dT) Pyrobaculum islandicum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.B7 Mg2+ the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+ Pyrobaculum islandicum
3.6.4.B7 Mn2+ the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+ Pyrobaculum islandicum

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.6.4.B7 guanidine-HCl the enzyme is stable up to 4.5 M guanidine hydrochloride Pyrobaculum islandicum

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.B7 Pyrobaculum islandicum Q9UWR5
-
-
3.6.4.B7 Pyrobaculum islandicum DSM 4184 Q9UWR5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.4.B7
-
 Pyrobaculum islandicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.B7 ATP + H2O the enzyme binds ssDNA, hydrolyzes ATP in a DNA-dependent manner and to catalyzes DNA strand exchange.It shows the ability to bind ssDNA and catalyze DNA strand exchange between ssDNA and homologous linear dsDNA. The ssDNA-dependent ATPase activity displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature Pyrobaculum islandicum ADP + phosphate
-
 ?
3.6.4.B7 ATP + H2O the enzyme binds ssDNA, hydrolyzes ATP in a DNA-dependent manner and to catalyzes DNA strand exchange.It shows the ability to bind ssDNA and catalyze DNA strand exchange between ssDNA and homologous linear dsDNA. The ssDNA-dependent ATPase activity displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature Pyrobaculum islandicum DSM 4184 ADP + phosphate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.4.B7 85
-
 the rate of the ATP hydrolysis increases with temperature up to 85°C, the maximum temperature at which the protein maintains its secondary structure Pyrobaculum islandicum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.6.4.B7 75
-
 the enzyme exhibits a biphasic Arrhenius plot of ATP hydrolysis with two characteristic energies of activation with a break point at 75°C. The activation energy below 75°C is higher than that above the break point. The cooperativity of ATP hydrolysis and ssDNA-binding ability of the protein above 75°C are greater than those at lower temperatures Pyrobaculum islandicum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.4.B7 25 87 the enzyme maintains its secondary structure and activities in vitro at high temperatures, up to 87°C. It also shows high stability of 18.3 kcal/mol at 25°C and neutral pH Pyrobaculum islandicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6.4.B7 0.013
-
 ATP pH 7.7, °C, 0.02 mM M13mp19dsDNA Pyrobaculum islandicum
3.6.4.B7 0.015
-
 ATP pH 7.7, 37°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.018
-
 ATP pH 7.7, 75°C, 0.02 mM DNA Pyrobaculum islandicum
3.6.4.B7 0.025
-
 ATP pH 7.7, 55°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.028
-
 ATP pH 7.7, 90°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.04
-
 ATP pH 7.7, 75°C, 0.02 mM poly(dA) Pyrobaculum islandicum
3.6.4.B7 0.042
-
 ATP pH 7.7, 65°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.048
-
 ATP pH 7.7, 70°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.052
-
 ATP pH 7.7, °C, 0.02 mM M13mp18ssDNA Pyrobaculum islandicum
3.6.4.B7 0.059
-
 ATP pH 7.7, 75°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.064
-
 ATP pH 7.7, 80°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.065
-
 ATP pH 7.7, 82°C, 0.02 mM poly(dT) Pyrobaculum islandicum
3.6.4.B7 0.067
-
 ATP pH 7.7, 75°C, 0.02 mM poly(dC) Pyrobaculum islandicum
3.6.4.B7 0.068
-
 ATP pH 7.7, 85°C, 0.02 mM poly(dT) Pyrobaculum islandicum