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Literature summary for 3.1.21.10 extracted from

  • Sharples, G.J.; Curtis, F.A.; McGlynn, P.; Bolt, E.L.
    Holliday junction binding and resolution by the Rap structure-specific endonuclease of phage lambda (2004), J. Mol. Biol., 340, 739-751.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli containing pMALc2 Lambdavirus lambda

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ minor junction cleavage Lambdavirus lambda
Mg2+ required for chi DNA cleavage, 0.1 mM is sufficient to promote stacking of the junction arms, at 1 mM no Rap-junction complexes were detected Lambdavirus lambda
Mn2+ required for chi DNA cleavage, reduced preference for cleavage in Mn2+ relative to Mg2+ on chi compared to small DNA substrates Lambdavirus lambda

Organism

Organism UniProt Comment Textmining
Lambdavirus lambda
-
-
-

Purification (Commentary)

Purification (Comment) Organism
amylose and heparin agarose chromatography of MBP-Rap, Rap29K, Rap-S and Rap17K Lambdavirus lambda

Storage Stability

Storage Stability Organism
-80°C, Tris-HCl buffer, 50% glycerol Lambdavirus lambda

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O Rap mediates symmetrical resolution of 50bp and chi Holliday structures containing larger homologous cores Lambdavirus lambda ?
-
?

Synonyms

Synonyms Comment Organism
RAP
-
Lambdavirus lambda