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Literature summary for 3.1.21.4 extracted from

  • Ohno, S.; Handa, N.; Watanabe-Matsui, M.; Takahashi, N.; Kobayashi, I.
    Maintenance forced by a restriction-modification system can be modulated by a region in its modification enzyme not essential for methyltransferase activity (2008), J. Bacteriol., 190, 2039-2049.
    View publication on PubMed
Search for more literature for 3.1.21.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BNH670 Escherichia coli

Protein Variants

Protein Variants Comment Organism
L80P the mutant enzyme shows decreased DNA methyltransferase activity at a higher temperature in vivo and in vitro than the wild type enzyme, the activity of the L80P mutant is completely lost at a high temperature Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P14633
-
-
Escherichia coli BNH2586 P14633
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O
-
 Escherichia coli double-stranded DNA fragments with terminal 5'-phosphates
-
 ?
DNA + H2O
-
 Escherichia coli BNH2586 double-stranded DNA fragments with terminal 5'-phosphates
-
 ?

Synonyms

Synonyms Comment Organism
EcoRII
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 42 the extract from cells expressing the wild type EcoRII shows the activity both at 30°C and 37°C, the extract from cells expressing the L80P mutant form shows activity at 30°C but not at 37°C, the L80P mutant protein is significantly unstable at 42°C compared with the wild type protein Escherichia coli