3.2.2.20: DNA-3-methyladenine glycosylase I

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For detailed information about DNA-3-methyladenine glycosylase I, go to the full flat file.

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

     3 Hydrolases

         3.2 Glycosylases

             3.2.2 Hydrolysing N-glycosyl compounds

                3.2.2.20 DNA-3-methyladenine glycosylase I

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Results	in table
4	Activating Compound
5842	AA Sequence
1	CAS Registry Number
18	Cloned(Commentary)
3	Cofactor
4	Crystallization (Commentary)
26	Disease/ Diagnostics
1	Expression
4	General Information
2	General Stability
5	IC50 Value
34	Inhibitors
1	Ki Value [mM]
2	KM Value [mM]
11	Metals/Ions
12	Molecular Weight [Da]
50	Natural Substrates/ Products (Substrates)
149	Organism
6	PDB ID
4	pH Optimum
1	pH Range
2	pI Value
17	Protein Variants
16	Purification (Commentary)
1	Reaction
1	Reaction Type
48	Reference
3	Source Tissue
3	Specific Activity [micromol/min/mg]
4	Storage Stability
95	Substrates and Products (Substrate)
3	Subunits
64	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
4	Temperature Stability [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.2.20 - DNA-3-methyladenine glycosylase I

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure resembling a catalytic intermediate complex. AlkC uses unique HEAT-like repeat folds and immunoglobulin-like domains to induce a sharp kink in the DNA, exposing the damaged nucleobase to active site residues that project into the DNA. The active site can accommodate and excise N3-methylcytosine and N1-methyladenine

2 entries

enzyme in unliganded form and in a ternary product complex with abasic DNA and 3-methyladenine. The abasic DNA is not flipped into the enzyme's active site, instead conformational relaxation must occur in the DNA upon base hydrolysis

Salmonella enterica subsp. enterica serovar Typhimurium

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679500

wild type and mutant enzyme Y16F in complex with 3-methyladenine, sitting drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.5, 1.8 M ammonium sulfate, 0.2 M Li2SO4

Staphylococcus aureus

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731077

structure resembling a catalytic intermediate complex. AlkC uses unique HEAT-like repeat folds and immunoglobulin-like domains to induce a sharp kink in the DNA, exposing the damaged nucleobase to active site residues that project into the DNA. The active site can accommodate and excise N3-methylcytosine and N1-methyladenine

Bacillus cereus

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750415

structure resembling a catalytic intermediate complex. AlkC uses unique HEAT-like repeat folds and immunoglobulin-like domains to induce a sharp kink in the DNA, exposing the damaged nucleobase to active site residues that project into the DNA. The active site can accommodate and excise N3-methylcytosine and N1-methyladenine

Pseudomonas fluorescens

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750415