Methylated-DNA—(protein)-cysteine S-methyltransferase
methylated-DNA-[protein]-cysteine S-methyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.63 | ||||||||
CAS no. | 77271-19-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) is an enzyme that catalyzes the chemical reaction
- DNA (containing 6-O-methylguanine) + protein L-cysteine DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine
Thus, the two substrates of this enzyme are DNA containing 6-O-methylguanine and protein L-cysteine, whereas its two products are DNA and protein S-methyl-L-cysteine. The S-methyl-L-cysteine residue irreversibly inactivates the protein, allowing only one transfer for each protein.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase.
Structural studies
[edit]As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1EH6, 1EH7, 1EH8, 1MGT, 1QNT, 1SFE, 1T38, 1T39, 1WRJ, 1YFH, and 2G7H.
References
[edit]- Foote RS, Mitra S, Pal BC (1980). "Demethylation of O6-methylguanine in a synthetic DNA polymer by an inducible activity in Escherichia coli". Biochem. Biophys. Res. Commun. 97 (2): 654–9. doi:10.1016/0006-291X(80)90314-9. PMID 7008792.
- Olsson M, Lindahl T (1980). "Repair of alkylated DNA in Escherichia coli. Methyl group transfer from O6-methylguanine to a protein cysteine residue". J. Biol. Chem. 255 (22): 10569–71. doi:10.1016/S0021-9258(19)70341-X. PMID 7000780.
- Pegg AE, Byers TL (1992). "Repair of DNA containing O6-alkylguanine". FASEB J. 6 (6): 2302–10. doi:10.1096/fasebj.6.6.1544541. PMID 1544541. S2CID 41168151.