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Literature summary for 2.1.1.72 extracted from

  • Beh, L.Y.; Debelouchina, G.T.; Clay, D.M.; Thompson, R.E.; Lindblad, K.A.; Hutton, E.R.; Bracht, J.R.; Sebra, R.P.; Muir, T.W.; Landweber, L.F.
    Identification of a DNA N6-adenine methyltransferase complex and its impact on chromatin organization (2019), Cell, 177, 1781-1796 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
macronucleus
-
Tetrahymena thermophila 31039
-
macronucleus
-
Oxytricha trifallax 31039
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + DNA adenine Tetrahymena thermophila the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?
S-adenosyl-L-methionine + DNA adenine Oxytricha trifallax the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?
S-adenosyl-L-methionine + DNA adenine Oxytricha trifallax JRB310 the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?
S-adenosyl-L-methionine + DNA adenine Tetrahymena thermophila SB210 the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?

Organism

Organism UniProt Comment Textmining
Oxytricha trifallax
-
-
-
Oxytricha trifallax JRB310
-
-
-
Tetrahymena thermophila
-
-
-
Tetrahymena thermophila SB210
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap Q column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration Tetrahymena thermophila
HiTrap Q column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration Oxytricha trifallax

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + DNA adenine the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA Tetrahymena thermophila S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?
S-adenosyl-L-methionine + DNA adenine the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA Oxytricha trifallax S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?
S-adenosyl-L-methionine + DNA adenine the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA Oxytricha trifallax JRB310 S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?
S-adenosyl-L-methionine + DNA adenine the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA Tetrahymena thermophila SB210 S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?

Synonyms

Synonyms Comment Organism
DNA 6mA methyltransferase
-
Tetrahymena thermophila
DNA 6mA methyltransferase
-
Oxytricha trifallax
MTA1 catalytic subunit Tetrahymena thermophila
MTA1 catalytic subunit Oxytricha trifallax
MTA1c
-
Tetrahymena thermophila
MTA1c
-
Oxytricha trifallax

General Information

General Information Comment Organism
malfunction enzyme gene disruption mutants fail to complete the sexual cycle when induced to mate and display complete lethality Tetrahymena thermophila
malfunction enzyme gene disruption mutants fail to complete the sexual cycle when induced to mate and display complete lethality Oxytricha trifallax