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Literature summary for 2.1.1.72 extracted from

  • Horton, J.R.; Liebert, K.; Hattman, S.; Jeltsch, A.; Cheng, X.
    Transition from nonspecific to specific DNA interactions along the substrate-recognition pathway of dam methyltransferase (2005), Cell, 121, 349-361.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.72

Protein Variants

Protein Variants Comment Organism
K139A site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme Escherichia coli
L122A site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme Escherichia coli
N120A site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme Escherichia coli
N120S site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme Escherichia coli
P134A site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme Escherichia coli
P134G site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme Escherichia coli
R124A site-directed mutagenesis, over 100fold reduced activity and about 10fold reduced DNA binding compared to the wild-type enzyme Escherichia coli
R137A site-directed mutagenesis, DNA binding is similar to the wild-type enzyme Escherichia coli
Y119A site-directed mutagenesis, over 100fold reduced activity compared to the wild-type enzyme, 2-3fold reduced DNA binding compared to the wild-type enzyme Escherichia coli
Y138A site-directed mutagenesis, DNA binding is similar to the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
sinefungin i.e. adenosyl ornithine, interaction mechanism with the enzyme, binding site structure, stabilization of the flipped adenine in presence of the inhibitor Tequatrovirus T4

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + DNA adenine Escherichia coli
-
 S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?
S-adenosyl-L-methionine + DNA adenine Tequatrovirus T4 specific target sequence is GATC S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Tequatrovirus T4
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information DNA substrate specificities of wild-type and mutant enzymes Tequatrovirus T4 ?
-
 ?
S-adenosyl-L-methionine + DNA adenine
-
 Escherichia coli S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?
S-adenosyl-L-methionine + DNA adenine specific target sequence is GATC Tequatrovirus T4 S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?
S-adenosyl-L-methionine + DNA adenine specific target sequence is GATC, transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved residues are M114, R116, P126, G128, R130, F111, S112, D171, K11, and Y174, overview, flipping of target adenine Tequatrovirus T4 S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?
S-adenosyl-L-methionine + DNA adenine transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved are Y119, N120, L122, R124, and P134, overview Escherichia coli S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?

Subunits

Subunits Comment Organism
More structure analysis of enzyme in ternary complex with partially and fully specific DNA and a methyl-donor analogue Escherichia coli
More structure analysis of enzyme in ternary complex with partially and fully specific DNA and S-adenosyl-L-homocysteine, S-adenosyl-L-methionine, or inhibitor adenosyl ornithine, i.e. sinefungin Tequatrovirus T4

Synonyms

Synonyms Comment Organism
DNA-adenine methyltransferase
-
 Escherichia coli
EcoDam
-
 Escherichia coli
T4 DNA-adenine methyltransferase
-
 Tequatrovirus T4
T4Dam
-
 Tequatrovirus T4