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Literature summary for 3.6.4.B7 extracted from

  • Kil, Y.V.; Glazunov, E.A.; Lanzov, V.A.
    Characteristic thermodependence of the RadA recombinase from the hyperthermophilic archaeon Desulfurococcus amylolyticus (2005), J. Bacteriol., 187, 2555-2557.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B7

Inhibitors

Inhibitors Comment Organism Structure
NaCl addition of 100 mM NaCl results in a 3.2-fold decrease of the monomer kcat value Desulfurococcus amylolyticus

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl 20 mM NaCl used in this mixture was found to be optimal for ATP hydrolysis Desulfurococcus amylolyticus

Organism

Organism UniProt Comment Textmining
Desulfurococcus amylolyticus Q9Y8J4
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O at optimal assay conditions, the RadADa presynaptic complex is able to hydrolyze ATP efficiently with ssDNA cofactors of 940 nt and greater. Circular and linearized M13 ssDNA demonstrate the same ability to stimulate ATP hydrolysis as a linearized dsDNA of this phage, whereas the supercoiled dsDNA (replicative form I) is a weak cofactor due to the only partial denaturation at 90°C Desulfurococcus amylolyticus ADP + phosphate
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Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
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 assay at Desulfurococcus amylolyticus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
80 102 preformation of presynaptic complex at 80°C guarantees the conservation of at least a part of the activity up to 102°C. Activity is close to zero at temperatures below 65°C Desulfurococcus amylolyticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
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 prerincubation of 0.015 mM enzyme for 6 min, complete inactivation of the protein Desulfurococcus amylolyticus
100
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 after boiling of 0.18 mM enzyme in 20 mM NaCl for 30 min, the enzyme retains one-third of its original activity. Two factors, preliminary presynaptic complex formation and high protein concentration, save, at least partially, the activity of RadADa protein, even at 100°C Desulfurococcus amylolyticus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.017
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 ATP pH 7.5, 90°C Desulfurococcus amylolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Desulfurococcus amylolyticus

General Information

General Information Comment Organism
physiological function the enzyme promotes recombination at temperatures approaching the DNA melting point Desulfurococcus amylolyticus