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Literature summary for 3.1.21.3 extracted from

  • Janscak, P.; Abadjieva, A.; Firman, K.
    The type I restriction endonuclease R.EcoR124I: Over-production and biochemical properties (1996), J. Mol. Biol., 257, 977-991.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
S-adenosyl-L-methionine stimulates, not required Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
DNA cleavage of DNA is inhibited by an increased degree of negative supercoiling Escherichia coli
S-adenosyl homocysteine competitive Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
290000 315000 pentameric enzyme form R2M2S1, gel filtration Escherichia coli
312000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
enzyme R.EcoR124I
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
duplex DNA + ATP the enzyme is both a restriction endonuclease and a modification methylase. Hemi-methylated DNA is the preferred substrate for methylation Escherichia coli double-stranded DNA fragments with terminal 5'-phosphate + ADP + inorganic phosphate
-
?
duplex DNA + ATP supercoiled with one or two SR124I recognition sites is cleaved by the same mechanism. Nicked-circle DNA is an intermediate of the cleavage reaction Escherichia coli double-stranded DNA fragments with terminal 5'-phosphate + ADP + inorganic phosphate
-
?

Subunits

Subunits Comment Organism
More the stoichiometry of R.EcoR124 appears to be R1M2S1, the stoichiometry of R.EcoKI is R2M2S1. S is the HsdS-subunit which is responsible for DNA recognition, R is HsdR-subunit which is required for restriction and M is an independent methyltransferase, Mtase Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
EcoB, methylase activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP required Escherichia coli