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Literature summary for 3.6.1.71 extracted from

  • Chauleau, M.; Jacewicz, A.; Shuman, S.
    DNA3pp5G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition (2015), Nucleic Acids Res., 43, 6075-6083.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure in complex with GMP, to 1.5 A resolution. GMP binds at the same position and in the same anti nucleoside conformation as AMP, and aprataxin makes more extensive nucleobase contacts with guanine than with adenine, via a hydrogen bonding network to the guanine O6, N1, N2 base edge Schizosaccharomyces pombe

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe O74859
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Schizosaccharomyces pombe ATCC 24843 O74859
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information aprataxin additionally is a DNA 3'-de-capping enzyme, converting DNAppG to DNA3'p and GMP, reaction of EC 3.1.12.2. Aprataxin hydrolyzes inosine and 6-O-methylguanosine caps, but not adeoxyguanosine cap Schizosaccharomyces pombe ?
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additional information aprataxin additionally is a DNA 3'-de-capping enzyme, converting DNAppG to DNA3'p and GMP, reaction of EC 3.1.12.2. Aprataxin hydrolyzes inosine and 6-O-methylguanosine caps, but not adeoxyguanosine cap Schizosaccharomyces pombe ATCC 24843 ?
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?

Synonyms

Synonyms Comment Organism
aprataxin
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Schizosaccharomyces pombe
HNT3
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Schizosaccharomyces pombe