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Literature summary for 4.2.99.18 extracted from

  • Lingaraju, G.M.; Prota, A.E.; Winkler, F.K.
    Mutational studies of Pa-AGOG DNA glycosylase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum (2009), DNA Repair, 8, 857-864.
    View publication on PubMed
Search for more literature for 4.2.99.18

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrobaculum aerophilum

Protein Variants

Protein Variants Comment Organism
D172N binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair Pyrobaculum aerophilum
D172Q binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair Pyrobaculum aerophilum
D172Q no detectable glycosylase activity Pyrobaculum aerophilum
K140Q binds to 8-oxoguanine containing single-stranded DNA more tightly than double-stranded DNA containing a 8-oxoguanine/cytosine base pair Pyrobaculum aerophilum
Q31E/D218S almost no glycosylase activity Pyrobaculum aerophilum
Q31S significantly reduced glycosylase activity Pyrobaculum aerophilum
W222A almost no glycosylase activity Pyrobaculum aerophilum
W222F mutant is similarly active as wild type on 8-oxoguanine/C substrates Pyrobaculum aerophilum
W69F mutant is similarly active as wild type on 8-oxoguanine/C substrates Pyrobaculum aerophilum

Organism

Organism UniProt Comment Textmining
Pyrobaculum aerophilum Q8ZVK6
-
-
Pyrobaculum aerophilum DSM 7523 Q8ZVK6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA with an abasic site
-
 Pyrobaculum aerophilum ?
-
 ?
DNA with an abasic site
-
 Pyrobaculum aerophilum DSM 7523 ?
-
 ?

Synonyms

Synonyms Comment Organism
Pa-AGOG DNA glycosylase bifunctional enzyme that catalyzes the excision of 8-oxoguanine by cleaving the N-glycosylic bond between the base and the deoxyribose moiety (glycosylase activity) and subsequently cleave the DNA backbone (lyase activity) Pyrobaculum aerophilum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
78
-
 Tm-value for mutant enzyme W69F Pyrobaculum aerophilum
84
-
 Tm-value for mutant enzyme D172Q Pyrobaculum aerophilum
86
-
 Tm-value for mutant enzyme Q31S Pyrobaculum aerophilum
87
-
 Tm-value for mutant enzyme Q31E/D218S Pyrobaculum aerophilum
87
-
 Tm-value for mutant enzyme W222A Pyrobaculum aerophilum
88
-
 Tm-value for mutant enzyme W222F Pyrobaculum aerophilum
93
-
 Tm-value for wild-type enzyme Pyrobaculum aerophilum