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Literature summary for 3.2.2.31 extracted from

  • Williams, S.D.; David, S.S.
    Formation of a Schiff base intermediate is not required for the adenine glycosylase activity of Escherichia coli MutY (1999), Biochemistry, 38, 15417-15424 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K142A the enzyme shows a dramatic decrease in the amount of enzyme-DNA cross-links with both 7,8-dihydro-8-oxo-2'-deoxyguanosine:adenine (less than 2%) and guanine:adenine (less than 2%) mispairs, despite having the ability to bind DNA and to catalyze apurinic site formation to the same extent as wild type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme catalyzes the removal of adenine bases mispaired with 2'-deoxyguanosine and 7,8-dihydro-8-oxo-2'-deoxyguanosine in DNA ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme catalyzes the removal of adenine bases mispaired with 2'-deoxyguanosine and 7,8-dihydro-8-oxo-2'-deoxyguanosine in DNA Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
? x * 39000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
mutY
-
Escherichia coli