Information on EC 2.1.1.63 - methylated-DNA-[protein]-cysteine S-methyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
2.1.1.63
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RECOMMENDED NAME
GeneOntology No.
methylated-DNA-[protein]-cysteine S-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase
This protein is involved in the repair of alkylated DNA. It acts only on the alkylated DNA (cf. EC 3.2.2.20, DNA-3-methyladenine glycosidase I and EC 3.2.2.21, DNA-3-methyladenine glycosidase II). This enzyme catalyses only one turnover and therefore is not strictly catalytic.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ada protein
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-
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AGAT
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AGT
Methanocaldococcus jannaschii P2
Q97VW7
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alkylguanine transferase
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alkylguanine transferase
Saccharomyces cerevisiae JD52
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-
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ATASE
Escherichia coli BS21
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-
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C-hAGT
-
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carboxyl terminal domain of the inducible Escherichia coli ada alkyltransferase
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methylated-DNA-[protein]-cysteine S-methyltransferase
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methylguanine DNA methyltransferase
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MGMT
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MGMT
P16455
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MGMT
Methanocaldococcus jannaschii P2
Q97VW7
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Mgt1
Saccharomyces cerevisiae JD52
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-
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N-hAGT
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O6-alkylguanine DNA alkyltransferase
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O6-alkylguanine DNA-alkyltransferase
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O6-alkylguanine-DNA alkyl-transferase
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O6-alkylguanine-DNA alkyltransferase
O67467
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O6-alkylguanine-DNA alkyltransferase
O27970
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O6-alkylguanine-DNA alkyltransferase
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-
O6-alkylguanine-DNA alkyltransferase
Escherichia coli BS21
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O6-alkylguanine-DNA alkyltransferase
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O6-alkylguanine-DNA alkyltransferase
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O6-alkylguanine-DNA alkyltransferase
-
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O6-alkylguanine-DNA alkyltransferase
-
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O6-alkylguanine-DNA alkyltransferase
Saccharomyces cerevisiae JD52
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O6-alkylguanine-DNA alkyltransferase
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O6-methylguanine DNA methyltransferase
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O6-methylguanine-DNA methyltransferase
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-
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O6-methylguanine-DNA methyltransferase
P16455
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O6-methylguanine-DNA methyltransferase
-
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O6-methylguanine-DNA methyltransferase
-
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O6-methylguanine-DNA methyltransferase
-
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O6-methylguanine-DNA methyltransferase
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O6-methylguanine-DNA-methyltransferase
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O6-MGMT
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O6meG-DNA alkyltransferase
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O6meG-DNA alkyltransferase
Saccharomyces cerevisiae JD52
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-
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OGT
Methanocaldococcus jannaschii P2
Q97VW7
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SSO2487
Methanocaldococcus jannaschii P2
Q97VW7
locus name
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SSO2487
Q97VW7
locus name
CAS REGISTRY NUMBER
COMMENTARY
77271-19-3
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Escherichia coli BS21
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-
-
Manually annotated by BRENDA team
three allelic variants: V1, V2, and V3
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-
Manually annotated by BRENDA team
Methanocaldococcus jannaschii P2
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SwissProt
Manually annotated by BRENDA team
C57BL/6 and F1 (C57BL/6 x 129/Sv) wild-type mice
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Manually annotated by BRENDA team
newborn C57bl/6 mice
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Manually annotated by BRENDA team
Pyrococcus sp. KOD1
KOD1
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Manually annotated by BRENDA team
Saccharomyces cerevisiae JD52
strain JD52
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Manually annotated by BRENDA team
strain HB8
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Manually annotated by BRENDA team
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cys acceptor site is buried in the protein and, in order for reaction with a DNA substrate to take place, a change in conformation of either the substrate or the protein must occur, Glu-172 and Asn-137 play a major structural role in the AGT protein
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crystals formed at 20C by conventional hanging drop-vapor diffusion method
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ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2,2,2-trifluoroethanol
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enzyme retains its native structure at high concentrations
2-propanol
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enzyme retains its native structure at high concentrations
Ethanol
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enzyme retains its native structure at high concentrations
Methanol
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enzyme retains its native structure at high concentrations
SDS
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enzyme retains its native structure at high concentrations
urea
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5 mM, melting temperature of wild-type enzyme: 91.5 C, melting temperature of mutant enzyme E83A: 89.2C, melting temperature of mutant enzyme E93A: 85.5C, melting temperature of mutant enzyme E158A: 90.6C, melting temperature of mutant enzyme E159A: 91.7 C
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
renaturation by dilution with buffer from 8 M urea or 6 M guanidine HCl instantly restores the secondary structure of the Ada protein to a state that is almost indistinguishable from the native state. Kinetics of renaturation is fast, at 0C the restoration is quantitative in less than 30 s. The heat-coagulated protein can be restored to full activity by cycling it through treatment with 8 M urea or 6 M guanidine
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