Cloned (Comment) | Organism |
---|---|
expression of C-terminally His-tagged wild-type NEIL3 in Escherichia coli, and expression of the C-terminally His-tagged glycosylase domain of Neil3, MmuNeil3DELTA324, in an Escherichia coli triple mutant lacking Fpg, Nei, and MutY glycosylase activities, the recombinant MmuNeil3 greatly reduced both the spontaneous mutation frequency and the level of FapyG in the DNA | Mus musculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics, overview | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | MmuNeil3 is a bifunctional DNA glycosylase that recognizes spiroiminodihydantoin and guanidinohydantoin, as well as 2,6-diamino-4-hydroxy-5-formamidopyrimidine, and 4,6-diamino-5-formamidopyrimidine, in double-stranded substrates. Neil3 greatly reduces both the spontaneous mutation frequency and the level of 2,6-diamino-4-hydroxy-5-formamidopyrimidine in the DNA. Substrate specificity of MmuNeil3 in vivo, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | MmuNeil3 is a bifunctional DNA glycosylase that recognizes spiroiminodihydantoin and guanidinohydantoin, as well as 2,6-diamino-4-hydroxy-5-formamidopyrimidine, and 4,6-diamino-5-formamidopyrimidine, in double-stranded substrates. Neil3 greatly reduces both the spontaneous mutation frequency and the level of 2,6-diamino-4-hydroxy-5-formamidopyrimidine in the DNA. Substrate specificity of MmuNeil3 in vivo, overview | Mus musculus | ? | - |
? | |
additional information | in duplex DNA, mouse Neil3 recognizes the oxidized purines, spiroiminodihydantoin, guanidinohydantoin, 2,6-diamino-4-hydroxy-5-formamidopyrimidine, and 4,6-diamino-5-formamidopyrimidine, but not 8-oxo-7,8-dihydroguanine. Neil3 prefers lesions in single-stranded DNA and in bubble structures. Mouse Neil3 forms a Schiff base intermediate via its N-terminal valine, in contrast to other enzyme of the family that use proline as nucleophile | Mus musculus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DNA glycosylase | - |
Mus musculus |
NEIL3 | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Mus musculus |
General Information | Comment | Organism |
---|---|---|
physiological function | Neil3 plays a role in repairing 2,6-diamino-4-hydroxy-5-formamidopyrimidine in vivo | Mus musculus |