Site-specific DNA-methyltransferase (adenine-specific)

Site-specific DNA-methyltransferase (adenine-specific)
Identifiers
EC number 2.1.1.72
CAS number 69553-52-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72, modification methylase, restriction-modification system) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + DNA adenine S-adenosyl-L-homocysteine + DNA 6-methylaminopurine

This is a large group of enzymes.[4]

The E. coli DNA adenine methyltransferase enzyme (Dam), is widely used for the chromatin profiling technique, DamID. In which the Dam is fused to a DNA-binding protein of interest and expressed as a transgene in a genetically tractable model organism to identify protein binding sites[5].

See also

References

  1. ↑ Kessler C, Manta V (August 1990). "Specificity of restriction endonucleases and DNA modification methyltransferases a review (Edition 3)". Gene. 92 (1–2): 1–248. doi:10.1016/0378-1119(90)90486-B. PMID 2172084.
  2. ↑ Roberts RJ (April 1990). "Restriction enzymes and their isoschizomers". Nucleic Acids Research. 18 Suppl: 2331–65. doi:10.1093/nar/18.suppl.2331. PMC 331877. PMID 2159140.
  3. ↑ Yuan R (1981). "Structure and mechanism of multifunctional restriction endonucleases". Annual Review of Biochemistry. 50: 285–319. doi:10.1146/annurev.bi.50.070181.001441. PMID 6267988.
  4. ↑ Roberts RJ. "A complete listing of all of these enzymes".
  5. ↑ Aughey GN, Southall TD (January 2016). "Dam it's good! DamID profiling of protein-DNA interactions". Wiley Interdisciplinary Reviews. Developmental Biology. 5 (1): 25–37. doi:10.1002/wdev.205. PMC 4737221. PMID 26383089.
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