Methylated-DNA—(protein)-cysteine S-methyltransferase
In enzymology, a methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) is an enzyme that catalyzes the chemical reaction
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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- 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
editAs 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.