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Information on EC 2.1.1.63 - methylated-DNA-[protein]-cysteine S-methyltransferase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97VW7

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EC Tree
IUBMB Comments
This protein is involved in the repair of methylated DNA. Unlike EC 3.2.2.20, DNA-3-methyladenine glycosidase I and EC 3.2.2.21, DNA-3-methyladenine glycosidase II, which remove the methylated base leaving an apurinic/apyrimidinic site, this enzyme transfers the methyl group from the methylated DNA to an internal cysteine residue, leaving an intact nucleotide. Since the methyl transfer is irreversible, the enzyme can only catalyse a single turnover.
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Saccharolobus solfataricus
UNIPROT: Q97VW7
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
o6-methylguanine-dna methyltransferase, atase, o6-alkylguanine-dna alkyltransferase, ada protein, o6-methylguanine dna methyltransferase, o6-methylguanine-dna-methyltransferase, o6-methylguanine methyltransferase, o6-alkylguanine dna alkyltransferase, o6-mgmt, methylguanine dna methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkylated DNA-protein alkyltransferase
-
Ada protein
-
-
-
-
MGMT
-
-
-
-
O6-methylguanine-DNA methyltransferase
-
-
-
-
O6-MGMT
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
DNA-6-O-methylguanine/DNA-4-O-methylthymine:[protein]-L-cysteine S-methyltransferase
This protein is involved in the repair of methylated DNA. Unlike EC 3.2.2.20, DNA-3-methyladenine glycosidase I and EC 3.2.2.21, DNA-3-methyladenine glycosidase II, which remove the methylated base leaving an apurinic/apyrimidinic site, this enzyme transfers the methyl group from the methylated DNA to an internal cysteine residue, leaving an intact nucleotide. Since the methyl transfer is irreversible, the enzyme can only catalyse a single turnover.
CAS REGISTRY NUMBER
COMMENTARY hide
77271-19-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DNA (containing 6-O-methylguanine) + [protein] L-cysteine
DNA (lacking 6-O-methylguanine) + protein S-methyl-L-cysteine
show the reaction diagram
-
-
-
?
DNA (containing 6-O-methylguanine) + [protein]-L-cysteine
DNA (without 6-O-methylguanine) + [protein]-S-methyl-L-cysteine
show the reaction diagram
-
-
-
?
SNAP-Vista Green + [protein]-L-cysteine
guanine + [protein]-S-Vista Green-L-cysteine
show the reaction diagram
fluorescent 6-O-benzylguanine derivative
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA (containing 6-O-methylguanine) + [protein] L-cysteine
DNA (lacking 6-O-methylguanine) + protein S-methyl-L-cysteine
show the reaction diagram
-
-
-
?
DNA (containing 6-O-methylguanine) + [protein]-L-cysteine
DNA (without 6-O-methylguanine) + [protein]-S-methyl-L-cysteine
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00077
DNA (containing 6-O-methylguanine)
pH 6.5, 50°C
0.01
SNAP-Vista Green
pH 6.5, 50°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.4
SNAP-Vista Green
pH 6.5, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17040
amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.35 M potassium nitrate and 1.6 M ammonium sulfate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C119F
the mutant shows reduced thermal stability compared to the wild type enzyme
C119L
the mutant shows reduced thermal stability compared to the wild type enzyme
D27A
the mutant shows reduced thermal stability compared to the wild type enzyme
D27K
the mutant shows reduced thermal stability compared to the wild type enzyme
additional information
the H5 variant harbouring five mutations (in the helix-turn helix motif) has a catalytic activity on O-6-benzyl guanine derivated substrates, whereas its ability to bind and repair the natural DNA containing 6-O-methylguanine is completely abolished
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
half life of 257 min
70
half life of 165 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very stable to proteases attack and detergents such as Triton X-100
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C stable for years
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologous expression by His-tag chromatography affinity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli ABLE-C cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Perugino, G.; Vettone, A.; Illiano, G.; Valenti, A.; Ferrara, M.C.; Rossi, M.; Ciaramella, M.
Activity and regulation of archaeal DNA alkyltransferase: conserved protein involved in repair of DNA alkylation damage
J. Biol. Chem.
287
4222-4231
2012
Saccharolobus solfataricus (Q97VW7), Saccharolobus solfataricus P2 (Q97VW7)
Manually annotated by BRENDA team
Perugino, G.; Miggiano, R.; Serpe, M.; Vettone, A.; Valenti, A.; Lahiri, S.; Rossi, F.; Rossi, M.; Rizzi, M.; Ciaramella, M.
Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein
Nucleic Acids Res.
43
8801-8816
2015
Saccharolobus solfataricus (Q97VW7), Saccharolobus solfataricus P2 (Q97VW7)
Manually annotated by BRENDA team