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Literature summary for 3.6.1.71 extracted from

  • Rass, U.; Ahel, I.; West, S.C.
    Actions of aprataxin in multiple DNA repair pathways (2007), J. Biol. Chem., 282, 9469-9474 .
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ binding of Aptx to duplex DNA is mediated by the C-terminal zinc finger domain, and efficient deadenylation requires the zinc finger Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
adenosine-5'-diphospho-5'-(ribonucleotide)-[DNA] + H2O Homo sapiens
-
AMP + 5'-phospho-(ribonucleotide)-[DNA]
-
?
adenosine-5'-diphospho-5'-[DNA] + H2O Homo sapiens
-
AMP + phospho-5'-[DNA]
-
?
additional information Homo sapiens aprataxin acts preferentially on adenylated nicks and double-strand breaks rather than on single-stranded DNA ?
-
?

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'-[DNA] + H2O
-
Homo sapiens AMP + phospho-5'-[DNA]
-
?
additional information aprataxin acts preferentially on adenylated nicks and double-strand breaks rather than on single-stranded DNA Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
APTX
-
Homo sapiens

General Information

General Information Comment Organism
physiological function the catalytic activity of Aptx resides within the HIT domain, the C-terminal zinc finger domain provides stabilizing contacts that lock the enzyme onto its high affinity AMP-DNA target site. Both domains are required for efficient AMP-DNA hydrolase activity. Aprataxin plays a role in base excision repair, specifically in the removal of adenylates that arise from abortive ligation reactions that take place at incised abasic sites in DNA Homo sapiens