Protein Variants | Comment | Organism |
---|---|---|
F110A | the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps | Escherichia coli |
F110W | the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | transient kinetics of Fpg | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | FPG excises oxidatively damaged purines in the base excision repair pathway, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene fpg | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
DNA containing ring-opened N7-methylguanine + H2O = deguanylated DNA + 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine | chemical reaction mechanism, overview. For the catalysis to occur, the damaged base must be extruded from the DNA helix and placed in the active site of enzyme, this is achieved in Fpg by kinking DNA at the lesion point. The reaction mechanism involves coupled conformational changes in the enzyme and DNA, which proceed sequentially and assemble the catalytic groups in the active site | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | FPG excises oxidatively damaged purines in the base excision repair pathway, overview | Escherichia coli | ? | - |
? | |
additional information | FPG excises oxidatively damaged purines in the base excision repair pathway, it acts on DNA containing 5,6-dihydrouracil, 8-oxo-7,8-dihydroguanine, or on apurinic/apyrimidinic DNA base pairs, analysis of conformational dynamics of Fpg protein and DNA substrates, rate constants of conformational transitions, and intrinsic mechanism of recognition and excision of damaged bases in DNA, overview | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | Fpg consists of two domains connected by a hinge polypeptide. The N-terminal domain contains a beta-sandwich core and a long alpha-helix with an N-terminal catalytic dyad, proline-glutamate. The C-terminal domain is mostly alpha-helical, containing two motifs almost universally conserved in Fpg proteins: a helix-two turn-helix motif and a beta-hairpin Cys4 zinc finger. The protein molecule possesses a positively charged cleft where damaged DNA is bound | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
formamidopyrimidine-DNA glycosylase | - |
Escherichia coli |
FPG | - |
Escherichia coli |
More | Fpg belongs to the class of DNA glycosylases/abasic site lyases | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | DNA glycosylases play a key role in the base excision repair pathway, Fpg belongs to the class of DNA glycosylases/abasic site lyases excising several oxidatively damaged purines in the base excision repair pathway | Escherichia coli |