EC |
2.1.1.113 |
Accepted name: |
site-specific DNA-methyltransferase (cytosine-N4-specific) |
Reaction: |
S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine |
Other name(s): |
modification methylase; restriction-modification system; DNA[cytosine-N4]methyltransferase; m4C-forming MTase; S-adenosyl-L-methionine:DNA-cytosine 4-N-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:DNA-cytosine N4-methyltransferase |
Comments: |
This is a large group of enzymes, most of which, with enzymes of similar site specificity listed as EC 3.1.21.3 (type 1 site-specific deoxyribonuclease), EC 3.1.21.4 (type II site-specific deoxyribonuclease) or EC 3.1.21.5 (type III site-specific deoxyribonuclease), form so-called ’restriction-modification systems’. A complete listing of all of these enzymes has been produced by R.J. Roberts and is available on-line at http://rebase.neb.com/rebase/rebase.html. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 169592-50-1 |
References: |
1. |
Kessler, C. and Manta, V. Specificity of restriction endonucleases and DNA modification methyltransferases: a review. Gene 92 (1990) 1–248. [DOI] [PMID: 2172084] |
2. |
Klimasauskas, S., Timinskas, A., Menkevicius, S., Butkiene, D., Butkus, V. and Janulaitis, A. Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5 DNA-methylases. Nucleic Acids Res. 17 (1989) 9823–9832. [DOI] [PMID: 2690010] |
3. |
Roberts, R.J. Restriction enzymes and their isoschizomers. Nucleic Acids Res. 18 (1990) 2331–2365. [PMID: 2159140] |
4. |
Yuan, R. Structure and mechanism of multifunctional restriction endonucleases. Annu. Rev. Biochem. 50 (1981) 285–319. [DOI] [PMID: 6267988] |
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[EC 2.1.1.113 created 1992] |
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