 | This article relies largely or entirely on a single source .(November 2020) |
| 3-methyl-adenine DNA glycosylase [Saccharomyces cerevisiae] | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | MAG1 | ||||||
| NCBI gene | 856885 | ||||||
| UniProt | P22134 | ||||||
| Other data | |||||||
| EC number | 3.2.2.21 | ||||||
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DNA-3-methyladenine glycosylase is an enzyme that in yeast is encoded by the MAG1 gene. [1]
MAG1 is involved in protecting DNA against alkylating agents. It initiates base excision repair by removing damaged bases to create abasic sites that are subsequently repaired. [1]
Deamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases.
DNA glycosylases are a family of enzymes involved in base excision repair, classified under EC number EC 3.2.2. Base excision repair is the mechanism by which damaged bases in DNA are removed and replaced. DNA glycosylases catalyze the first step of this process. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. This is accomplished by flipping the damaged base out of the double helix followed by cleavage of the N-glycosidic bond.
In biochemistry and molecular genetics, an AP site, also known as an abasic site, is a location in DNA that has neither a purine nor a pyrimidine base, either spontaneously or due to DNA damage. It has been estimated that under physiological conditions 10,000 apurinic sites and 500 apyrimidinic may be generated in a cell daily.
Base excision repair (BER) is a cellular mechanism, studied in the fields of biochemistry and genetics, that repairs damaged DNA throughout the cell cycle. It is responsible primarily for removing small, non-helix-distorting base lesions from the genome. The related nucleotide excision repair pathway repairs bulky helix-distorting lesions. BER is important for removing damaged bases that could otherwise cause mutations by mispairing or lead to breaks in DNA during replication. BER is initiated by DNA glycosylases, which recognize and remove specific damaged or inappropriate bases, forming AP sites. These are then cleaved by an AP endonuclease. The resulting single-strand break can then be processed by either short-patch or long-patch BER.
MUTYH is a human gene that encodes a DNA glycosylase, MUTYH glycosylase. It is involved in oxidative DNA damage repair and is part of the base excision repair pathway. The enzyme excises adenine bases from the DNA backbone at sites where adenine is inappropriately paired with guanine, cytosine, or 8-oxo-7,8-dihydroguanine, a common form of oxidative DNA damage.
8-Oxoguanine glycosylase, also known as OGG1 is a DNA glycosylase enzyme that, in humans, is encoded by the OGG1 gene. It is involved in base excision repair. It is found in bacterial, archaeal and eukaryotic species.
UV excision repair protein RAD23 homolog B is a protein that in humans is encoded by the RAD23B gene.
Uracil-DNA glycosylase is also known as UNG or UDG. Its most important function is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosidic bond and initiating the base-excision repair (BER) pathway.
Cyclin-O is a protein that in humans is encoded by the CCNO gene.
G/T mismatch-specific thymine DNA glycosylase is an enzyme that in humans is encoded by the TDG gene. Several bacterial proteins have strong sequence homology with this protein.
DNA-3-methyladenine glycosylase also known as 3-alkyladenine DNA glycosylase (AAG) or N-methylpurine DNA glycosylase (MPG) is an enzyme that in humans is encoded by the MPG gene.
Endonuclease III-like protein 1 is an enzyme that in humans is encoded by the NTHL1 gene.
Endonuclease VIII-like 1 is an enzyme that in humans is encoded by the NEIL1 gene.
Methyl-CpG-binding domain protein 4 is a protein that in humans is encoded by the MBD4 gene.
Endonuclease VIII-like 2 is an enzyme that in humans is encoded by the NEIL2 gene.
Single-strand selective monofunctional uracil DNA glycosylase is an enzyme that in humans is encoded by the SMUG1 gene. SMUG1 is a glycosylase that removes uracil from single- and double-stranded DNA in nuclear chromatin, thus contributing to base excision repair.
8-Oxo-2'-deoxyguanosine (8-oxo-dG) is an oxidized derivative of deoxyguanosine. 8-Oxo-dG is one of the major products of DNA oxidation. Concentrations of 8-oxo-dG within a cell are a measurement of oxidative stress.
Nei endonuclease VIII-like 3 is a protein in humans that is encoded by the NEIL3 gene.
DNA-3-methyladenine glycosylase II is an enzyme that catalyses the following chemical reaction:
DNA-formamidopyrimidine glycosylase is an enzyme with systematic name DNA glycohydrolase . FPG is a base excision repair enzyme which recognizes and removes a wide range of oxidized purines from correspondingly damaged DNA. It was discovered by Zimbabwean scientist Christopher J. Chetsanga in 1975.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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