Literature summary for 2.1.1.63 extracted from

Hazra, T.K.; Roy, R.; Biswas, T.; Grabowski, D.T.; Pegg, A.E.; Mitra, S.
Specific recognition of O6-methylguanine in DNA by active site mutants of human O6-methylguanine-DNA methyltransferase (1997), Biochemistry, 36, 5769-5776.

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Protein Variants

Protein Variants	Comment	Organism
C145A	inactive mutant enzyme forms a specific and stable complex with a 6-O-methylguanine-containing oligonucleotide substrate	Homo sapiens
C145S	inactive mutant enzyme forms a specific and stable complex with a 6-O-methylguanine-containing oligonucleotide substrate	Homo sapiens
additional information	deletion of more than 8 or 31 residues from the amino or carboxyl terminus, respectively, leads to the loss of both activity and substrate binding. Removal of Arg9 or Leu176 and distal residues inactivates the protein	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the alkyl group is transferred without a cofactor to Cys145 residue of the enzyme and thereby inactivates the protein	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA containing 6-O-methylguanine + [protein]-L-cysteine	the alkyl group is transferred without a cofactor to Cys145 residue of the enzyme and thereby inactivates the protein	Homo sapiens	DNA lacking 6-O-methylguanine + [protein]-S-methyl-L-cysteine	-	?

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Release 2023.1 (January 2023)