Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.4.B7 extracted from

  • Qian, X.; He, Y.; Luo, Y.
    Binding of a second magnesium is required for ATPase activity of RadA from Methanococcus voltae (2007), Biochemistry, 46, 5855-5863.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Methanococcus voltae

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Methanococcus voltae

Protein Variants

Protein Variants Comment Organism
D246A loss of binding a second Mg2+. Initial ATP turnover rate is reduced by about 20-fold Methanococcus voltae
D246N initial ATP turnover rate is reduced by about 20-fold Methanococcus voltae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for ATPase activity. The enzyme contains a secondary Mg2+ site as well as a canonical P-loop and nucleotide-lined primary Mg2+ site. The secondary Mg2+ site is important for modulating the ATPase activity Methanococcus voltae

Organism

Organism UniProt Comment Textmining
Methanococcus voltae O73948
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O single-stranded DNA-dependent ATPase Methanococcus voltae ADP + phosphate
-
?

Synonyms

Synonyms Comment Organism
MvRadA
-
Methanococcus voltae

General Information

General Information Comment Organism
physiological function play a key role in DNA repair by forming helical nucleoprotein filaments which promote a hallmark strand exchange reaction between homologous DNA substrates Methanococcus voltae