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Literature summary for 3.1.21.4 extracted from

  • Takahashi, S.; Matsuno, H.; Furusawa, H.; Okahata, Y.
    Direct monitoring of allosteric recognition of type IIE restriction endonuclease EcoRII (2008), J. Biol. Chem., 283, 15023-15030.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.21.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain JM109 Escherichia coli

Protein Variants

Protein Variants Comment Organism
K263A inactive mutant with truncated EcoRII N-domain Escherichia coli
R330A inactive mutant with truncated EcoRII C-domain Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ in the presence of Ca2+ ions, EcoRII binds to the target DNA but does not cleave the DNA strand Escherichia coli
Mg2+ required Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap heparin column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O EcoRII recognizes two units of recognition sequences (5'-CCWGG-3') included in one DNA chain (cis-binding) or in two DNA chains one by one (trans-binding), and cleaves either site Escherichia coli double-stranded DNA fragments with terminal 5'-phosphates
-
 ?
additional information no activity is observed using 1-site DNA as substrate Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
EcoRII
-
 Escherichia coli
type IIE restriction endonuclease
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.018
-
 DNA wild type enzyme with 2-site DNA Escherichia coli