From Wikipedia, the free encyclopedia
DNA-formamidopyrimidine glycosylase
Identifiers
EC no. 3.2.2.23
CAS no. 78783-53-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

DNA-formamidopyrimidine glycosylase ( EC 3.2.2.23, Fapy-DNA glycosylase, deoxyribonucleate glycosidase, 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase, 2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase, formamidopyrimidine-DNA glycosylase, DNA-formamidopyrimidine glycosidase, Fpg protein) is an enzyme with systematic name DNA glycohydrolase (2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing). [1] FPG is a base excision repair enzyme which recognizes and removes a wide range of oxidized purines from correspondingly damaged DNA. [2] It was discovered by Zimbabwean scientist Christopher J. Chetsanga in 1975. [3]

This enzyme catalyses the following chemical reaction

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine

This enzyme participates in processes leading to recovery from mutagenesis and/or cell death by alkylating agents.

References

  1. ^ Boiteux S, O'Connor TR, Laval J (October 1987). "Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein". The EMBO Journal. 6 (10): 3177–83. PMC  553760. PMID  3319582.
  2. ^ Serre1; Pereira De Jésus, K; Boiteux, S; Zelwer, C; Castaing, B; et al. (2002). "Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA". The EMBO Journal. 21 (12): 2854–2865. doi: 10.1093/emboj/cdf304. PMC  126059. PMID  12065399.{{ cite journal}}: CS1 maint: numeric names: authors list ( link)
  3. ^ Chetsanga C.J., Lindahl T. (1979). "Release of 7-methylguanine residues whose imidazole rings have been opened from damaged DNA by a DNA glycosylase from Escherichia coli". Nucleic Acids Res. 6 (11): 3673–84. doi: 10.1093/nar/6.11.3673. PMC  327965. PMID  386277.

External links

From Wikipedia, the free encyclopedia
DNA-formamidopyrimidine glycosylase
Identifiers
EC no. 3.2.2.23
CAS no. 78783-53-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

DNA-formamidopyrimidine glycosylase ( EC 3.2.2.23, Fapy-DNA glycosylase, deoxyribonucleate glycosidase, 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase, 2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase, formamidopyrimidine-DNA glycosylase, DNA-formamidopyrimidine glycosidase, Fpg protein) is an enzyme with systematic name DNA glycohydrolase (2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing). [1] FPG is a base excision repair enzyme which recognizes and removes a wide range of oxidized purines from correspondingly damaged DNA. [2] It was discovered by Zimbabwean scientist Christopher J. Chetsanga in 1975. [3]

This enzyme catalyses the following chemical reaction

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine

This enzyme participates in processes leading to recovery from mutagenesis and/or cell death by alkylating agents.

References

  1. ^ Boiteux S, O'Connor TR, Laval J (October 1987). "Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein". The EMBO Journal. 6 (10): 3177–83. PMC  553760. PMID  3319582.
  2. ^ Serre1; Pereira De Jésus, K; Boiteux, S; Zelwer, C; Castaing, B; et al. (2002). "Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA". The EMBO Journal. 21 (12): 2854–2865. doi: 10.1093/emboj/cdf304. PMC  126059. PMID  12065399.{{ cite journal}}: CS1 maint: numeric names: authors list ( link)
  3. ^ Chetsanga C.J., Lindahl T. (1979). "Release of 7-methylguanine residues whose imidazole rings have been opened from damaged DNA by a DNA glycosylase from Escherichia coli". Nucleic Acids Res. 6 (11): 3673–84. doi: 10.1093/nar/6.11.3673. PMC  327965. PMID  386277.

External links


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