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Literature summary for 3.6.4.B7 extracted from

  • Kil, Y.V.; Baitin, D.M.; Masui, R.; Bonch-Osmolovskaya, E.A.; Kuramitsu, S.; Lanzov, V.A.
    Efficient strand transfer by the RadA recombinase from the hyperthermophilic archaeon Desulfurococcus amylolyticus (2000), J. Bacteriol., 182, 130-134.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
overexpressed in Escherichia coli Desulfurococcus amylolyticus

Organism

Organism UniProt Comment Textmining
Desulfurococcus amylolyticus Q9Y8J4
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Desulfurococcus amylolyticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the highly purified enzyme exusively catalyzes single-stranded DNA-dependent ATP hydrolysis, which monitors presynaptic recombinational complex formation, at temperatures above 65°C. The RadA protein alone efficiently promotes the strand exchange reaction at the range of temperatures from 80 to 90°C, i.e., at temperatures approaching the melting point of DNA Desulfurococcus amylolyticus ADP + phosphate
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 ?

Synonyms

Synonyms Comment Organism
RadA
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 Desulfurococcus amylolyticus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2 2.5 ATP pH 7.6, 80-95°C, the RadADa ATP hydrolysis shows monomer kcat values of 1.2 to 2.5 per min at the temperature interval 80 to 95°C Desulfurococcus amylolyticus