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Literature summary for 2.1.1.37 extracted from

  • Pradhan, S.; Roberts, R.J.
    Hybrid mouse-prokaryotic DNA (cytosine-5) methyltransferases retain the specificity of the parental C-terminal domain (2000), EMBO J., 19, 2103-2114.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
construction of three hybrid methyltransferases, containing the intact N-terminus of the murine Dnmt1 and most of the coding sequences from M.HhaI (GCGC), M.HpaII (CCGG) or M.SssI (CG). The hybrids are biologically active when expressed in a baculovirus system and show the specificity of the parental C-terminal domain Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-values for hybrid enzymes Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
170000
-
 hybrid enzymes Dnmt1-HhaI and Dnmt1-HpaII Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Dnmt1-HhaI and Dnmt1-HpaII hybrid enzymes Mus musculus

Storage Stability

Storage Stability Organism
-20°C, hybrid enzymes Dnmt1-HhaI and Dnmt1-HpaII are stable for several weeks Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + DNA
-
 Mus musculus S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover-numbers for hybrid enzymes Mus musculus