3.2.2.20: DNA-3-methyladenine glycosylase I
This is an abbreviated version!
For detailed information about DNA-3-methyladenine glycosylase I, go to the full flat file.
Word Map on EC 3.2.2.20
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3.2.2.20
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glycosylases
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abasic
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excises
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self-labeling
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1,n6-ethenoadenine
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snap-tagged
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3-methylguanine
- 3.2.2.20
- glycosylases
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abasic
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excises
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self-labeling
- 1,n6-ethenoadenine
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snap-tagged
- 3-methylguanine
Reaction
Synonyms
3-MeA DNA glycosylase I, 3-methyl adenine DNA glycosylase I, 3-methyladenine DNA glycosylase, 3-methyladenine DNA glycosylase I, 3MeA, 3MeA DNA glycosylase, AAG, Aag 3MeA DNA glycosylase, AlkC, AlkD, APNG, APNG DNA glycosylase, bAag, deoxyribonucleate 3-methyladenine DNA glycosidase I, DNA-3-methyladenine DNA glycosidase I, GI, human m3A DNA glycosylase, m3A DNA glycosylase I, MAG, MAG1, Mag1 3-methyladenine DNA glycosylase, Mag1p, Mag2p, MPG, MpgI, N3-methyladenine DNA glycosylase, protein Tag, TAG, TagA, TagA protein, TagI, Yx1J
ECTree
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Engineering
Engineering on EC 3.2.2.20 - DNA-3-methyladenine glycosylase I
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D170N
Saccharomyces pombe
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the mutation substantially decreases enzymatic activity without abolishing it
I147V/T151A/A206S
Saccharomyces pombe
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the mutant retains base excision activity toward alkylated DNA substrates, but its level of activity is decreased compared to the wild type
K126N/E130G/N175D
Saccharomyces pombe
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the mutant retains base excision activity toward alkylated DNA substrates, but its level of activity is decreased compared to the wild type
L122M
Saccharomyces pombe
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the mutant retains base excision activity toward alkylated DNA substrates, but its level of activity is decreased compared to the wild type
N42Y/V165A
Saccharomyces pombe
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the mutant retains base excision activity toward alkylated DNA substrates, but its level of activity is decreased compared to the wild type
R149K
Saccharomyces pombe
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the mutant retains base excision activity toward alkylated DNA substrates, but its level of activity is decreased compared to the wild type
additional information
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construction of a truncated DELTA80AAG enzyme mutant, substrate specificity in comparison to the wild-type enzyme shows that both the full-length and truncated AAG excise 1,N2-ethenoguanine, albeit weakly, from duplex DNA, while uracil is excised from both single- and double-stranded DNA, but only by full-length AAG, single-turnover excision kinetics, overview