Oxoguanine glycosylase

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8-oxoguanine DNA glycosylase

PDB rendering based on 1ebm.

Available structures: 1ebm, 1fn7, 1hu0, 1ko9, 1lwv, 1lww, 1lwy, 1m3h, 1m3q, 1n39, 1n3a, 1n3c, 1yqk, 1yql, 1yqm, 1yqr, 2i5w, 2nob, 2noe, 2nof, 2noh, 2noi, 2nol, 2noz

Identifiers

Symbol(s)

OGG1; HMMH; HOGG1; MUTM; OGH1

External IDs

OMIM: 601982 MGI: 1097693 HomoloGene: 1909

Gene ontology
Molecular Function:	• damaged DNA binding • endonuclease activity • oxidized purine base lesion DNA N-glycosylase activity • hydrolase activity, acting on glycosyl bonds • lyase activity
Cellular Component:	• cellular_component • intracellular • nucleus • nucleoplasm • mitochondrion
Biological Process:	• base-excision repair • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002542 (mRNA)
NP_002533 (protein)

NM_010957 (mRNA)
NP_035087 (protein)

Location

Chr 3: 9.77 - 9.78 Mb

Chr 6: 113.29 - 113.3 Mb

Pubmed search

[1]

[2]

8-oxoguanine glycosylase is a DNA glycosylase enzyme. It is involved in base excision repair.

It is the primary enzyme responsible for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which occurs as a result of exposure to reactive oxygen species (ROS). The action of this enzyme includes lyase activity for chain cleavage. Alternative splicing of the C-terminal region of this gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence. Type 1 alternative splice variants end with exon 7 and type 2 end with exon 8. All variants share the N-terminal region in common. Many alternative splice variants for this gene have been described, but the full-length nature for every variant has not been determined. The N-terminus of this gene contains a mitochondrial targetting signal, essential for mitochondrial localization.^[1]

[edit] References

^ Entrez Gene: OGG1 8-oxoguanine DNA glycosylase.

[edit] Further reading

Boiteux S, Radicella JP (2000). "The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis.". Arch. Biochem. Biophys. 377 (1): 1–8. doi:10.1006/abbi.2000.1773. PMID 10775435.
Park J, Chen L, Tockman MS, et al. (2004). "The human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) DNA repair enzyme and its association with lung cancer risk.". Pharmacogenetics 14 (2): 103–9. PMID 15077011.
Hung RJ, Hall J, Brennan P, Boffetta P (2006). "Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review.". Am. J. Epidemiol. 162 (10): 925–42. doi:10.1093/aje/kwi318. PMID 16221808.

[edit] External links

MeSH oxoguanine+glycosylase+1,+human

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v • d • e Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases	Amylase (Alpha-Amylase) - Chitinase - Lysozyme - Neuraminidase - Galactosidases (Alpha, Beta) - alpha-Mannosidase - Glucuronidase - Hyaluronidase - Pullulanase - Glucocerebrosidase - Galactosylceramidase - Alpha-N-acetylgalactosaminidase - Alpha-N-acetylglucosaminidase - Fucosidase - Hexosaminidase (HEXA, HEXB) - Iduronidase Disaccharidase (Sucrase/Sucrase-isomaltase/Invertase, Maltase, Trehalase, Lactase) Glucosidases (Cellulase, Alpha-glucosidase, Beta-glucosidase, Debranching enzyme)

3.2.2: Hydrolysing N-Glycosyl compounds	DNA glycosylases: Oxoguanine glycosylase