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Literature summary for 3.2.2.21 extracted from

  • Wang, P.; Guliaev, A.B.; Hang, B.
    Metal inhibition of human N-methylpurine-DNA glycosylase activity in base excision repair (2006), Toxicol. Lett., 166, 237-247.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ inhibitory above 0.05 mM. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate Homo sapiens
Ni2+ inhibitory above 0.05 mM, but to lesser extent than Cd2+ or Zn2+. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate Homo sapiens
Zn2+ enzyme active site has a potential binding site for Zn2+. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P29372
-
-

Renatured (Commentary)

Renatured (Comment) Organism
inhibition by Cd2+, Ni2+, or Zn2+ can be reversed by EDTA Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
duplex oligonucleotide substrate containing ethenoadenine + H2O
-
Homo sapiens ethenoadenine + oligonucleotide
-
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