EC |
3.2.2.23 |
Accepted name: |
DNA-formamidopyrimidine glycosylase |
Reaction: |
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine |
Other name(s): |
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 |
Systematic name: |
DNA glycohydrolase [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing] |
Comments: |
May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 78783-53-6 |
References: |
1. |
Boiteux, S., O'Connor, T.R. and Laval, J. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. EMBO J. 6 (1987) 3177–3183. [PMID: 3319582] |
|
[EC 3.2.2.23 created 1990, modified 2000] |
|
|
|
|
EC |
3.2.2.31 |
Accepted name: |
adenine glycosylase |
Reaction: |
Hydrolyses free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site. |
Other name(s): |
mutY (gene name); A/G-specific adenine glycosylase |
Systematic name: |
adenine-DNA deoxyribohydrolase (adenine-releasing) |
Comments: |
The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA. The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity. After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break. In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Au, K.G., Clark, S., Miller, J.H. and Modrich, P. Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. USA 86 (1989) 8877–8881. [DOI] [PMID: 2682664] |
2. |
Michaels, M.L., Tchou, J., Grollman, A.P. and Miller, J.H. A repair system for 8-oxo-7,8-dihydrodeoxyguanine. Biochemistry 31 (1992) 10964–10968. [PMID: 1445834] |
|
[EC 3.2.2.31 created 2018] |
|
|
|
|
EC |
3.5.4.32 |
Accepted name: |
8-oxoguanine deaminase |
Reaction: |
8-oxoguanine + H2O = urate + NH3 |
Glossary: |
8-oxoguanine = 2-amino-7,9-dihydro-1H-purine-6,8-dione |
Other name(s): |
8-OGD |
Systematic name: |
8-oxoguanine aminohydrolase |
Comments: |
Zn2+ is bound in the active site. 8-Oxoguanine is formed via the oxidation of guanine within DNA by reactive oxygen species. If uncorrected, this modification leads to the incorporation of 8-oxoG:A mismatches and eventually to G:C to T:A transversions.
|
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hall, R.S., Fedorov, A.A., Marti-Arbona, R., Fedorov, E.V., Kolb, P., Sauder, J.M., Burley, S.K., Shoichet, B.K., Almo, S.C. and Raushel, F.M. The hunt for 8-oxoguanine deaminase. J. Am. Chem. Soc. 132 (2010) 1762–1763. [DOI] [PMID: 20088583] |
|
[EC 3.5.4.32 created 2012] |
|
|
|
|
EC |
3.6.1.55 |
Accepted name: |
8-oxo-dGTP diphosphatase |
Reaction: |
8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate |
Glossary: |
8-oxo-dGTP = 8-oxo-7,8-dihydro-2′-deoxyguanosine 5′-triphosphate |
Other name(s): |
MutT; 7,8-dihydro-8-oxoguanine triphosphatase; 8-oxo-dGTPase; 7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase |
Systematic name: |
8-oxo-dGTP diphosphohydrolase |
Comments: |
This enzyme hydrolyses the phosphoanhydride bond between the α and β phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA. It does not hydrolyse 2-hydroxy-dATP (cf. EC 3.6.1.56, 2-hydroxy-dATP diphosphatase) [4]. Requires Mg2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ito, R., Hayakawa, H., Sekiguchi, M. and Ishibashi, T. Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools. Biochemistry 44 (2005) 6670–6674. [DOI] [PMID: 15850400] |
2. |
Yoshimura, K., Ogawa, T., Ueda, Y. and Shigeoka, S. AtNUDX1, an 8-oxo-7,8-dihydro-2′-deoxyguanosine 5′-triphosphate pyrophosphohydrolase, is responsible for eliminating oxidized nucleotides in Arabidopsis. Plant Cell Physiol. 48 (2007) 1438–1449. [DOI] [PMID: 17804481] |
3. |
Nakamura, T., Meshitsuka, S., Kitagawa, S., Abe, N., Yamada, J., Ishino, T., Nakano, H., Tsuzuki, T., Doi, T., Kobayashi, Y., Fujii, S., Sekiguchi, M. and Yamagata, Y. Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base. J. Biol. Chem. 285 (2010) 444–452. [DOI] [PMID: 19864691] |
4. |
Yonekura, S., Sanada, U. and Zhang-Akiyama, Q.M. CiMutT, an asidian MutT homologue, has a 7, 8-dihydro-8-oxo-dGTP pyrophosphohydrolase activity responsible for sanitization of oxidized nucleotides in Ciona intestinalis. Genes Genet. Syst. 85 (2010) 287–295. [PMID: 21178309] |
|
[EC 3.6.1.55 created 2011] |
|
|
|
|