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

BRENDA support

2.1.1.72: site-specific DNA-methyltransferase (adenine-specific)

This is an abbreviated version!
For detailed information about site-specific DNA-methyltransferase (adenine-specific), go to the full flat file.

Word Map on EC 2.1.1.72

Reaction

S-adenosyl-L-methionine
+
adenine in DNA
=
S-adenosyl-L-homocysteine
+
N6-methyladenine in DNA

Synonyms

6mA DNA methyltransferases, A1S_0222, AamA, acinetobacter adenine methyltransferase A, adenine methyltransferase, adenine methyltransferase 1, adenine N6-methyltransferase, adenine-(N6)-DNA methyltransferase, adenine-N6 DNA methyltransferase, adenine-N6 MTAse, AhdI methyltransferase, AMT1, ApyPI, AquII, AquIII, AquIV, BamHI MTase, BsbI, C18A3.1, CcrM, CcrM DNA adenine methyltransferase, CcrM methylase, CdpI, cell cycle-regulated DNA methyltransferase, cell cycle-regulated methyltransferase, cell-cycle regulating MTase, CstMI, Dam, Dam DNA-(adenine-N6)-methyltransferase, Dam DNA-(adenine-N6)-MTase, Dam methylase, Dam MTase, DAMT-1, DANN 6mA MTase, DNA 6mA methyltransferase, DNA adenine 5'-GATC-3' methylase, DNA adenine methylase, DNA adenine methyltransferase, DNA adenine methyltransferases, DNA adenine MTase, DNA adenine N6-methyltransferase, DNA adenine-N6 MTase, DNA methyltransferase, DNA MTase, DNA N-6 adenine methyltransferase, DNA N6 adenine methyltransferase 1, DNA N6-adenine methyltransferase, DNA [amino]-methyltransferase, DNA-(adenine N6)-methyltransferase, DNA-(adenine-N6)-methyltransferase, DNA-(adenine-N6-)-methyltransferase, DNA-(N6-adenine)-methyltransferase, DNA-adenine methyltransferase, DNA-[adenine] methyltransferase, DNA-[adenine] MTase, DNA-[N6-adenine] MTase, DNA-[N6-adenine]-methyltransferase, DNA:m6A MTase, DNAm6A MTase, DraRI, DrdIV, EcoDam, EcoDam DNA-[N6-adenine] MTase, EcoKDam, EcoP15I, EcoP15I MTase, EcoRII DNA methyltransferase, EcoRV, EcoVIII, gamma-adenine MTase, Hia5 protein, Hin1523 protein, HP0050 methyltransferase, HP0593 DNA-(N6-adenine)-methyltransferase, HP0593 MTase, HpyAXII, HpyIIIM, isospecific adenine DNA methyltransferase, isospecific DNA MTase, KpnI DNA methyltransferase, KpnI DNA-(N6-adenine)-methyltransferase, KpnI MTase, M-RsrI, M. TthP, M.Aba17978ORF8565P, M.AbaBGORF222P, M.AluBI, M.BseCI, M.BstZ1II, M.Csp231I, M.DpnM, M.EcaI, M.EcoKCcrM, M.EcoP15I, M.EcoRI, M.EcoRII, M.EcoRV, M.EcoVIII, M.EfaBMDam, M.HindIII, M.HpyAXII, M.KpnI, M.LlaCI, M.MboIIA, M.NgoAXP, M.RsrI, M.TaqI, M1.HpyAVI, M1.MboII, M2.BstSEI, m6A methyltransferase, MaqI, MettL3-MettL14 complex, MmeI, modification methylase, More, MTA1, MTA1c, MTase, N-6 adenine-specific DNA methyltransferase 1, N6 adenine methyltransferase, N6 adenine MTase, N6-Ade MTase, N6-adenine DNA -methyltransferase, N6-adenine methyltransferase, N6-adenine MTase, N6AMT1, N6_N4_MTase, NgoAXPMod subunit, NhaXI, NlaCI, Nme1821 protein, NmeAIII, Pho(M98A)Dam, PlaDI, PspOMII, PspPRI, RceI, restriction-modification system, RpaB5I, RsrI N6-adenine DNA methyltransferase, SdeAI, sequence-specific DNA adenine methyltransferase, specific methyltransferase, SpoDI, T4 Dam, T4 Dam (N6-Ade)-MTase, T4 Dam DNA methyltransferase, T4 Dam DNA-(N6-adenine)-methyltransferase, T4 Dam MTase, T4 DNA-adenine methyltransferase, T4Dam, T4Dam DNA-[N6-adenine] MTase, T4DNA-(N6-adenine)-methyltransferase, type IC M.EcoR124I DNA methyltransferase, VspI methyltransferase, Wadmtase, [N6-adenine] MTase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.72 site-specific DNA-methyltransferase (adenine-specific)

Crystallization

Crystallization on EC 2.1.1.72 - site-specific DNA-methyltransferase (adenine-specific)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with double-stranded DNA containing the recognition sequence GANTC, sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.8, with 10% (w/v) polyethylene glycol 8000 and 3% (w/v) polyethylene glycol 6000
enzyme complexed with substrate S-adenosyl-L-methionine, product S-adenosyl-L-homocysteine, or inhibitor sinefungin, and L72P mutant apo-enzyme, 2.0 mg/ml protein in crystallization buffer containing 100 mM HEPES, pH 7.4, 1.5 M LiSO4, and 1-20 mM of the ligand compounds, X-ray diffraction structure determination and analysis at 2.3 A resolution
in complex with cognate DNA at 1.89 A resolution, in the presence of S-adenosyl-L-homocysteine
in complex with duplex DNA and AMP, hanging drop vapor diffusion method, using 10% (w/v) PEG 5000 monomethyl ether, 0.1 M HEPES pH 7.5, 0.2M potassium acetate and 15 mM MnCl2 at 20°C
-
in complex with non-cognate DNA, lacking any GATC sequences, hanging drop vapor diffusion method, using 5-40% (w/v) PEG 200 from and 100 mM MES or HEPES (pH 6.4-7.0)
in complex with its cognate DNA, by the hanging-drop vapour-diffusion method, to a resolution of 2.5 A, crystals belong to the hexagonal space group P6
apoenzyme, hanging drop vapor diffusion method, using 1.0 M Bis-Tris, pH 9.0, 1.4 M ammonium tartrate. Enzyme in complex with S-adenosyl-L-methionine, hanging drop vapor diffusion method, using 1.0 M Bis-Tris pH 6.0, 14% (w/v) PEG 2000, 0.2 M lithium sulfate
-
purified recombinant enzyme in binary complex with S-adenosyl-L-homocysteine or in ternary complex with a synthetic 12 bp DNA duplex and S-adenosyl-L-homocysteine, hanging drop vapour diffusion method, 16°C, reservoir solution contains 2.4 M ammonium sulfate and 100 mM MES, pH 6.0, for the binary complex, and contains 20-25% w/v PEG 8000, 100 mM HEPES, pH 7.5, and 10 mM ammonium sulfate for the ternary complex, X-ray diffraction structure determination and analysis at 2.3-3.5 A resolution, modeling
Tequatrovirus T4
in complex with S-adenosyl-L-methionine, S-adenosyl-L-homocysteine and with the inhibitor sinefungin, at a resolution of 2.4 A