EC number:2.1.1.37

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.37
Description:DNA (cytosine-5-)-methyltransferase.
Alternative Name: Type II DNA methylase.
Site-specific DNA-methyltransferase (cytosine-specific).
Restriction-modification system.
Modification methylase.
Methylphosphotriester-DNA methyltransferase.
DNA-cytosine methyltransferase.
DNA-cytosine 5-methylase.
DNA transmethylase.
DNA methyltransferase.
DNA methylase.
DNA cytosine methylase.
DNA cytosine C(5) methylase.
DNA 5-cytosine methylase.
Deoxyribonucleic methylase.
Deoxyribonucleic acid modification methylase.
Deoxyribonucleic acid methyltransferase.
Deoxyribonucleic acid methylase.
Deoxyribonucleic acid (cytosine-5-)-methyltransferase.
Deoxyribonucleic (cytosine-5-)-methyltransferase.
Deoxyribonucleate methyltransferase.
Deoxyribonucleate methylase.
Cytosine-specific DNA methyltransferase.
Cytosine DNA methyltransferase.
Cytosine DNA methylase.
Cytosine 5-methyltransferase.
Prosite: PDOC00089;
PDB:
PDBScop
6FDF 8062267; 8062268; 8062267; 8062268; 8062267; 8062268; 8062267; 8062268;
5GUT 8053022; 8053023; 8053025; 8053027; 8053021; 8053026;
4DA4 8053021; 8053022; 8053023; 8053025; 8053026; 8053027; 8053021; 8053022; 8053023; 8053025; 8053026; 8053027;
5GUV 8053021; 8053022; 8053023; 8053025; 8053026; 8053027;
3PT9 8053021; 8053022; 8053023; 8053025; 8053026; 8053027;
 » show all
Cath: 1.10.10.2230; 1.10.720.50; 3.90.120.10; 3.90.120.20; 2.20.70.90; 2.30.30.140; 2.30.30.490; 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.37
BRENDA Enzyme Link: BRENDA 2.1.1.37
KEGG Enzyme Link: KEGG2.1.1.37
BioCyc Enzyme Link: BioCyc 2.1.1.37
ExPASy Enzyme Link: ExPASy2.1.1.37
EC2PDB Enzyme Link: EC2PDB 2.1.1.37
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.37
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.37
IntEnz Enzyme Link: IntEnz 2.1.1.37
MEDLINE Enzyme Link: MEDLINE 2.1.1.37

EC number:2.1.1.37

MSA:

2.1.1.37;
Phylogenetic Tree:

2.1.1.37;
Uniprot:
M-CSA:
RHEA:13681 a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
CXXC domain of human DNMT1 is essential for enzymatic activity.Pradhan M, Estève PO, Chin HG, Samaranayke M, Kim GD, Pradhan S2008 Sep 2318754681
The Polycomb group protein EZH2 directly controls DNA methylation.Viré E, Brenner C, Deplus R, Blanchon L, Fraga M, Didelot C, Morey L, Van Eynde A, Bernard D, Vanderwinden JM, Bollen M, Esteller M, Di Croce L, de Launoit Y, Fuks F2006 Feb 1616357870