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Literature summary extracted from

  • Skorvaga, M.; Raven, N.D.; Margison, G.P.
    Thermostable archaeal O6-alkylguanine-DNA alkyltransferases (1998), Proc. Natl. Acad. Sci. USA, 95, 6711-6715.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.63 O6-methylguanine oligonucleotide preincubation of extracts with a short oligonucleotide containing a single O6-methylguanine residue causes essentially complete loss of ATase activity Homo sapiens
2.1.1.63 O6-methylguanine oligonucleotide preincubation of extracts with a short oligonucleotide containing a single O6-methylguanine residue causes essentially complete loss of ATase activity Pyrobaculum islandicum
2.1.1.63 O6-methylguanine oligonucleotide preincubation of extracts with a short oligonucleotide containing a single O6-methylguanine residue causes essentially complete loss of ATase activity Pyrococcus furiosus
2.1.1.63 O6-methylguanine oligonucleotide preincubation of extracts with a short oligonucleotide containing a single O6-methylguanine residue causes essentially complete loss of ATase activity Sulfolobus acidocaldarius
2.1.1.63 O6-methylguanine oligonucleotide preincubation of extracts with a short oligonucleotide containing a single O6-methylguanine residue causes essentially complete loss of ATase activity Thermococcus litoralis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.63 15000
-
 x * 15000, SDS-PAGE Pyrobaculum islandicum
2.1.1.63 16000
-
 x * 16000, SDS-PAGE Sulfolobus acidocaldarius
2.1.1.63 22000
-
 x * 22000, SDS-PAGE Pyrococcus furiosus
2.1.1.63 23000
-
 x * 23000, SDS-PAGE Thermococcus litoralis
2.1.1.63 24000
-
 x * 24000, SDS-PAGE Homo sapiens
2.1.1.63 39000
-
 x * 39000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine Escherichia coli the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine Homo sapiens the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine Pyrococcus furiosus the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine Sulfolobus acidocaldarius the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine Thermococcus litoralis the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine Pyrobaculum islandicum the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ?
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine Escherichia coli BS21 the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.63 Escherichia coli
-
-
-
2.1.1.63 Escherichia coli BS21
-
-
-
2.1.1.63 Homo sapiens
-
-
-
2.1.1.63 Pyrobaculum islandicum
-
-
-
2.1.1.63 Pyrococcus furiosus
-
-
-
2.1.1.63 Sulfolobus acidocaldarius
-
-
-
2.1.1.63 Thermococcus litoralis
-
-
-

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
-
 Escherichia coli DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine
-
 Homo sapiens DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine
-
 Pyrococcus furiosus DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine
-
 Sulfolobus acidocaldarius DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine
-
 Thermococcus litoralis DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine
-
 Pyrobaculum islandicum DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Escherichia coli DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Homo sapiens DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Pyrococcus furiosus DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Sulfolobus acidocaldarius DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Thermococcus litoralis DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Pyrobaculum islandicum DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ?
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine
-
 Escherichia coli BS21 DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir
2.1.1.63 DNA (containing 6-O-methylguanine) + [protein] L-cysteine the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Escherichia coli BS21 DNA (without 6-O-methylguanine) + [protein] S-methyl-L-cysteine
-
 ir

Subunits

EC Number Subunits Comment Organism
2.1.1.63 ? x * 16000, SDS-PAGE Sulfolobus acidocaldarius
2.1.1.63 ? x * 39000, SDS-PAGE Escherichia coli
2.1.1.63 ? x * 24000, SDS-PAGE Homo sapiens
2.1.1.63 ? x * 23000, SDS-PAGE Thermococcus litoralis
2.1.1.63 ? x * 22000, SDS-PAGE Pyrococcus furiosus
2.1.1.63 ? x * 15000, SDS-PAGE Pyrobaculum islandicum

Synonyms

EC Number Synonyms Comment Organism
2.1.1.63 ATASE
-
 Escherichia coli
2.1.1.63 ATASE
-
 Homo sapiens
2.1.1.63 ATASE
-
 Pyrococcus furiosus
2.1.1.63 ATASE
-
 Sulfolobus acidocaldarius
2.1.1.63 ATASE
-
 Thermococcus litoralis
2.1.1.63 ATASE
-
 Pyrobaculum islandicum
2.1.1.63 O6-alkylguanine-DNA alkyltransferase
-
 Escherichia coli
2.1.1.63 O6-alkylguanine-DNA alkyltransferase
-
 Homo sapiens
2.1.1.63 O6-alkylguanine-DNA alkyltransferase
-
 Pyrococcus furiosus
2.1.1.63 O6-alkylguanine-DNA alkyltransferase
-
 Sulfolobus acidocaldarius
2.1.1.63 O6-alkylguanine-DNA alkyltransferase
-
 Thermococcus litoralis
2.1.1.63 O6-alkylguanine-DNA alkyltransferase
-
 Pyrobaculum islandicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.63 37
-
-
 Escherichia coli
2.1.1.63 37
-
-
 Homo sapiens
2.1.1.63 75
-
-
 Sulfolobus acidocaldarius
2.1.1.63 90
-
-
 Thermococcus litoralis
2.1.1.63 100
-
-
 Pyrococcus furiosus
2.1.1.63 100
-
-
 Pyrobaculum islandicum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.1.63 50 100 activity increases from 50°C to 100%, 60°C: about 45% of the activity at 100°C, 50% about 15% of maximal activity Pyrococcus furiosus
2.1.1.63 60 100 activity at 60°C is about 35% of the activity at 100°C Pyrobaculum islandicum
2.1.1.63 65 85 65°C: about 50% of maximal activity, 85°C: about 45% of maximal activity Sulfolobus acidocaldarius

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.1.63 37
-
 t1/2: 32 h Sulfolobus acidocaldarius
2.1.1.63 37
-
 t1/2: 38 h Pyrobaculum islandicum
2.1.1.63 37
-
 t1/2: 60 h Pyrococcus furiosus
2.1.1.63 37
-
 t1/2: 72 h Thermococcus litoralis
2.1.1.63 60
-
 t1/2: 18 h Thermococcus litoralis
2.1.1.63 60
-
 t1/2: 12 h Pyrobaculum islandicum
2.1.1.63 60
-
 t1/2: 16 h Sulfolobus acidocaldarius
2.1.1.63 60
-
 t1/2: 40 h Pyrococcus furiosus
2.1.1.63 80
-
 t1/2: 0.5 h Sulfolobus acidocaldarius
2.1.1.63 80
-
 t1/2: 13 h Thermococcus litoralis
2.1.1.63 80
-
 t1/2: 5 h Pyrococcus furiosus
2.1.1.63 80
-
 t1/2: 5.5 h Pyrobaculum islandicum

General Information

EC Number General Information Comment Organism
2.1.1.63 physiological function the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Escherichia coli
2.1.1.63 physiological function the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Homo sapiens
2.1.1.63 physiological function the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Pyrococcus furiosus
2.1.1.63 physiological function the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Sulfolobus acidocaldarius
2.1.1.63 physiological function the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Thermococcus litoralis
2.1.1.63 physiological function the DNA repair protein O6-alkylguanine-DNA alkyltransferase is a principal mechanism of cellular resistance to the toxic and mutagenic effects of DNA damage produced by certain monofunctional alkylating agents. ATase operates by the transfer of the offending alkyl groups from the O6 position of guanine and the O4 position of thymine in damaged DNA to a cysteine residue at the active site of the protein. This is an irreversible process that results in the stoichiometric inactivation of the protein Pyrobaculum islandicum