Literature summary for 2.1.1.72 extracted from

Malygin, E.G.; Evdokimov, A.A.; Zinoviev, V.V.; Ovechkina, L.G.; Lindstrom, W.M.; Reich, N.O.; Schlagman, S.L.; Hattman, S.
A dual role for substrate S-adenosyl-L-methionine in the methylation reaction with bacteriophage T4 Dam DNA-[N6-adenine]-methyltransferase (2001), Nucleic Acids Res., 29, 2361-2369.

Search for more literature for 2.1.1.72

Organism

Organism	UniProt	Comment	Textmining
Tequatrovirus T4	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + DNA adenine	in unmethylated target (2A/A duplex), the enzyme alone randomly binds to the asymetric 2A/A duplex, S-adenosyl-L-methionine induces an allosteric T4 conformational change that promotes reorientation of the enzyme to the strand containing the native base. S-Adenosyl-L-methionine increases enzyme binding-specificity, in addition to serving as the methyl donor, the enzyme recognizes the palindromic sequence GATC	Tequatrovirus T4	S-adenosyl-L-homocysteine + DNA 6-methylaminopurine	-	?

Synonyms

Synonyms	Comment	Organism
T4 Dam (N6-Ade)-MTase	-	Tequatrovirus T4

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)