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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.4.B7
-
 Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.B7 Mg2+ ATP hydrolysis is not detected in presence of Mg2+ Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.4.B7 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

EC Number Organism UniProt Comment Textmining
3.6.4.B7 Archaeoglobus fulgidus O29269
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.4.B7
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.B7 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
-
 ?
3.6.4.B7 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

EC Number Subunits Comment Organism
3.6.4.B7 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.4.B7 60 70
-
 Archaeoglobus fulgidus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.6.4.B7 50 80 50°C: about 40% of maximal activity, 80°C: about 60% of maximal activity Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.4.B7 7.5
-
 assay at Archaeoglobus fulgidus