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Literature summary for 3.2.2.31 extracted from

  • Chepanoske, C.L.; Golinelli, M.P.; Williams, S.D.; David, S.S.
    Positively charged residues within the iron-sulfur cluster loop of E. coli MutY participate in damage recognition and removal (2000), Arch. Biochem. Biophys., 380, 11-19 .
    View publication on PubMed
Search for more literature for 3.2.2.31

Protein Variants

Protein Variants Comment Organism
K196A the mutant enzyme exhibits a slight reduction of the rate of adenine removal from a G:A base pair-containing duplex compared to the wild type enzyme Escherichia coli
K198A the mutant enzyme exhibits a significant reduction (15fold) of the rate of adenine removal from a G:A base pair-containing duplex compared to the wild type enzyme Escherichia coli
R194A the mutant shows wild type activity 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 is specific for adenine removal from 7,8-dihydro-8-oxoguanine:adenine as well as guanine:adenine, and cytosine:adenine mispairs in double-stranded DNA ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P17802
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is specific for adenine removal from 7,8-dihydro-8-oxoguanine:adenine as well as guanine:adenine, and cytosine:adenine mispairs in double-stranded DNA Escherichia coli ?
-
 ?
additional information substrate recognition is evaluated using a DNA duplex containing a 2'-deoxyadenosine analog in a base pair opposite guanine or 7,8-dihydro-8-oxoguanine Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
mutY
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 Escherichia coli