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Literature summary for 3.1.21.10 extracted from

  • Iwasaki, H.; Takahagi, M.; Shiba, T.; Nakata, A.; Shinagawa, H.
    Escherichia coli RuvC protein is an endonuclease that resolves the holliday structure (1991), EMBO J., 10, 4381-4389.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ cannot replace Mn2+ Escherichia coli
Mg2+ required for activation Escherichia coli
Zn2+ cannot replace Mn2+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19000
-
2 * 19000 Escherichia coli
40000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DNA + H2O Escherichia coli holliday structure hydrolyzed DNA
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
highly purified, 99% pure Escherichia coli
RuvC Escherichia coli

Storage Stability

Storage Stability Organism
-20°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O at low concentrations the enzyme binds preferentially to the junction, in high concentrations it binds nonspecifically to any part of the DNA Escherichia coli hydrolyzed DNA
-
?
DNA + H2O DNA topology rather than a sequence determine the cleavage site Escherichia coli hydrolyzed DNA
-
?
DNA + H2O nicks the ssDNA strands across the junction at symmetrical positions within the homologous arms Escherichia coli hydrolyzed DNA
-
?
DNA + H2O holliday structure Escherichia coli hydrolyzed DNA
-
?

Subunits

Subunits Comment Organism
dimer homodimer Escherichia coli
dimer 2 * 19000 Escherichia coli