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Literature summary 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.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.63 C145A inactive mutant enzyme forms a specific and stable complex with a 6-O-methylguanine-containing oligonucleotide substrate Homo sapiens
2.1.1.63 C145S inactive mutant enzyme forms a specific and stable complex with a 6-O-methylguanine-containing oligonucleotide substrate Homo sapiens
2.1.1.63 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

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

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.63 Homo sapiens
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.63 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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