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

BRENDA support

Literature summary for 3.6.4.B7 extracted from

  • McIlwraith, M.J.; Hall, D.R.; Stasiak, A.Z.; Stasiak, A.; Wigley, D.B.; West, S.C.
    RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination (2001), Nucleic Acids Res., 29, 4509-4517.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B7

Cloned(Commentary)

Cloned (Comment) Organism
-
 Archaeoglobus fulgidus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ ATP hydrolysis is not detected in presence of Mg2+ Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Archaeoglobus fulgidus the enzyme catalyses efficient D-loop formation and strand exchange at temperatures of 60-70°C, capable of promoting strand transfer through at least 1200 bp of duplex DNA AMP + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus O29269
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the enzyme catalyses efficient D-loop formation and strand exchange at temperatures of 60-70°C, capable of promoting strand transfer through at least 1200 bp of duplex DNA Archaeoglobus fulgidus AMP + diphosphate
-
 ?
ATP + H2O ATPase activity is most efficient in presence of ssDNA, it is considerably reduced in presence of dsDNA and virtually no ATP is hydrolysed in absence of DNA. The enzyme catalyses efficient D-loop formation and strand exchange at temperatures of 60-70°C, capable of promoting strand transfer through at least 1200 bp of duplex DNA Archaeoglobus fulgidus AMP + diphosphate
-
 ?

Subunits

Subunits Comment Organism
oligomer the enzyme forms rings and nucleoprotein filaments. In the presence of ssDNA and ATP-gamma-S helical nucleoprotein filament structures are observed. RadA forms filaments on ssDNA. No protein-DNA complexes are formed on dsDNA. Such preference for binding ssDNA may allow targeting of RadA protein to the ssDNA. In absence of DNA, RadA shows a tendency to form ring-like structures in vivo. Ring structures may be the inactive storage form of the recombinase that are transported to the sites of DNA repair and then converted into functional helical nucleoprotein filaments when loaded onto ssDNA Archaeoglobus fulgidus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60 70
-
 Archaeoglobus fulgidus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 80 50°C: about 40% of maximal activity, 80°C: about 60% of maximal activity Archaeoglobus fulgidus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Archaeoglobus fulgidus