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Literature summary for 3.1.21.4 extracted from

  • Tamulaitis, G.; Mucke, M.; Siksnys, V.
    Biochemical and mutational analysis of EcoRII functional domains reveals evolutionary links between restriction enzymes (2006), FEBS Lett., 580, 1665-1671.
    View publication on PubMed
Search for more literature for 3.1.21.4

Protein Variants

Protein Variants Comment Organism
D299A no catalytic activity, mutant like wild-type remains in dimeric form Escherichia coli
D329A less than 0.01% residual activity, mutant like wild-type remains in dimeric form Escherichia coli
E271A no catalytic activity, mutant like wild-type remains in dimeric form Escherichia coli
E337A less than 0.01% residual activity, mutant like wild-type remains in dimeric form Escherichia coli
K324A no catalytic activity, mutant like wild-type remains in dimeric form Escherichia coli
K328A less than 0.01% residual activity, mutant like wild-type remains in dimeric form Escherichia coli
R330A no catalytic activity, mutant like wild-type remains in dimeric form Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
 2 * 26000, calculated Escherichia coli
54000 57000 gel-filtration, wild-type and mutants Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 isoform EcoRII
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O
-
 Escherichia coli ? the isolated C-terminal domain dimer has an interface that binds a single cognate DNA molecule whereas the N-terminal domain is a monomer that also binds a single copy of cognate DNA ?

Subunits

Subunits Comment Organism
dimer 2 * 26000, calculated Escherichia coli
additional information the isolated C-terminal domain dimer has an interface that binds a single cognate DNA molecule whereas the N-terminal domain is a monomer that also binds a single copy of cognate DNA Escherichia coli