Biology:Site-specific DNA-methyltransferase (adenine-specific)

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Site-specific DNA-methyltransferase (adenine-specific)
Identifiers
EC number2.1.1.72
CAS number69553-52-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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. "Specificity of restriction endonucleases and DNA modification methyltransferases a review (Edition 3)". Gene 92 (1–2): 1–248. August 1990. doi:10.1016/0378-1119(90)90486-B. PMID 2172084. 
  2. "Restriction enzymes and their isoschizomers". Nucleic Acids Research 18 Suppl: 2331–65. April 1990. doi:10.1093/nar/18.suppl.2331. PMID 2159140. 
  3. "Structure and mechanism of multifunctional restriction endonucleases". Annual Review of Biochemistry 50: 285–319. 1981. doi:10.1146/annurev.bi.50.070181.001441. PMID 6267988. 
  4. "The Restriction Enzyme Database". http://rebase.neb.com/rebase/rebase.html. 
  5. "Dam it's good! DamID profiling of protein-DNA interactions". Wiley Interdisciplinary Reviews: Developmental Biology 5 (1): 25–37. January 2016. doi:10.1002/wdev.205. PMID 26383089. 

External links