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Literature summary for 3.6.1.71 extracted from

  • Rass, U.; Ahel, I.; West, S.C.
    Molecular mechanism of DNA deadenylation by the neurological disease protein aprataxin (2008), J. Biol. Chem., 283, 33994-34001 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.71

Protein Variants

Protein Variants Comment Organism
H201A mutant displays weak activity Homo sapiens
H258A mutant displays substantial residual activity Homo sapiens
H260A no detectable activity Homo sapiens
H262A mutant displays weak activity Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
additional information DNA deadenylation activity is metal-independent Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q7Z2E3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine-5'-diphospho-5'-(ribonucleotide)-[DNA] + H2O
-
 Homo sapiens AMP + 5'-phospho-(ribonucleotide)-[DNA]
-
 ?
adenosine-5'-diphospho-5'-[5'-AGATTATCTTCGAGCTAC-3'] + H2O
-
 Homo sapiens AMP + phospho-5'-[5'-AGATTATCTTCGAGCTAC-3']
-
 ?
adenosine-5'-diphospho-5'-[5'-ATTCCGATAGTGACTACA-3'] + H2O
-
 Homo sapiens AMP + phospho-5'-[5'-ATTCCGATAGTGACTACA-3']
-
 ?
adenosine-5'-diphospho-5'-[5'-CATATCCGTGTCGCCCTCATTCCGATAGTGACTACA-3'] + H2O
-
 Homo sapiens AMP + phospho-5'-[5'-CATATCCGTGTCGCCCTCATTCCGATAGTGACTACA-3']
-
 ?
adenosine-5'-diphospho-5'-[5'-GTAGCTCGAAGATAATCTGAGGGCGACACGGATATG-3'] + H2O
-
 Homo sapiens AMP + phospho-5'-[5'-GTAGCTCGAAGATAATCTGAGGGCGACACGGATATG-3']
-
 ?
adenosine-5'-diphospho-5'-[5'-TGTAGTCACTATCGGAATGAGGGCGACACGGATATG-3'] + H2O
-
 Homo sapiens AMP + phospho-5'-[5'-TGTAGTCACTATCGGAATGAGGGCGACACGGATATG-3']
-
 ?
adenosine-5'-diphospho-5'-[DNA] + H2O
-
 Homo sapiens AMP + phospho-5'-[DNA]
-
 ?
additional information the target of APTX ares 5'-adenylates at DNA nicks or breaks that result from abortive DNA ligation reactions Homo sapiens ?
-
 ?

General Information

General Information Comment Organism
physiological function APTX acts as a nick sensor. When an adenylated nick is encountered by APTX, base pairing at the 5' terminus of the nick is disrupted as the adenylate is accepted into the active site of the enzyme. Adenylate removal occurs by a two-step process that proceeds through a transient AMP-APTX covalent intermediate Homo sapiens