Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Liebert, K.; Hermann, A.; Schlickenrieder, M.; Jeltsch, A.
    Stopped-flow and mutational analysis of base flipping by the Escherichia coli Dam DNA-(adenine-N6)-methyltransferase (2004), J. Mol. Biol., 341, 443-454.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.72 expression of wild-type and mutant enzymes Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.72 D181A site-directed mutagenesis, inactive mutant, mutation abolishes base flipping, D181 seems to contact and stabilize the flipped base, i.e. the intermediate state of the base flipping process Escherichia coli
2.1.1.72 S188A site-directed mutagenesis, exchange in the loop next to the active site, 7-8fold reduction of kcat, mutant shows 92% of wild-type enzyme activity Escherichia coli
2.1.1.72 T190A site-directed mutagenesis, mutant shows 75% of wild-type enzyme activity Escherichia coli
2.1.1.72 Y184A site-directed mutagenesis, mutant shows 1.7% of wild-type enzyme activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.72 additional information
-
additional information quantitative stopped-flow kinetics using 2-aminopurine as a probe to detect base flipping, wild-type and mutant enzymes Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.72 S-adenosyl-L-methionine + DNA adenine Escherichia coli
-
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.72 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.72 recombinant wild-type and mutant enzymes to over 95% purity Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.72 S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA D181 and Y184 are essential for activity Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.72 additional information substrate specificity with different oligonucleotides, substrate binding specificity, overview Escherichia coli ?
-
?
2.1.1.72 S-adenosyl-L-methionine + DNA adenine
-
Escherichia coli S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
?
2.1.1.72 S-adenosyl-L-methionine + DNA adenine required substrate recognition target sequence is GATC, occuring base flipping in absence of S-adenosyl-L-methionine is a biphasic process and very fast, but binding of the flipped base into the active site pocket requiring S-adenosyl-L-methionine is slow, active site contains the conserved DPPY motif, whose tyrosine184 residue stacks to the flipped target base Escherichia coli S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
?

Subunits

EC Number Subunits Comment Organism
2.1.1.72 More secondary structure analysis Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.1.1.72 Dam DNA-(adenine-N6)-methyltransferase
-
Escherichia coli
2.1.1.72 Dam DNA-(adenine-N6)-MTase
-
Escherichia coli
2.1.1.72 EcoDam
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.72 37
-
assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.72 additional information
-
additional information
-
Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.72 7.5
-
assay at Escherichia coli