Matches in DBpedia 2016-04 for { ?s ?p "AlkD (Alkylpurine glycosylase D) is an enzyme belonging to a family of DNA glycosylases that are involved in DNA repair. It was discovered by a team of Norwegian biologists from Oslo in 2006. It was isolated from a soil-dwelling Gram-positive bacteria Bacillus cereus, along with another enzyme AlkC. AlkC and AlkD are most probably derived from the same protein as indicated by their close resemblance. They are also found in other prokaryotes. Among eukaryotes, they are found only in the single-celled species only, such as Entamoeba histolytica and Dictyostelium discoideum. The enzyme specifically targets 7mG (methyl-guanine) in the DNA, and is, therefore, unique among DNA glycosylases. It can also act on other methylpurines with less affinity. It indicates that the enzyme is specific for locating and cutting (excision) of chemically modified bases from DNA, exactly at 7mG, whenever there are errors in replication. It accelerates the rate of 7mG hydrolysis 100-fold over the spontaneous depurination. Thus, it protects the genome from harmful changes induced by chemical and environmental agents. Its crystal structure was described in 2008. It is the first HEAT repeat protein identified to interact with nucleic acids or to contain enzymatic activity."@en }
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- AlkD abstract "AlkD (Alkylpurine glycosylase D) is an enzyme belonging to a family of DNA glycosylases that are involved in DNA repair. It was discovered by a team of Norwegian biologists from Oslo in 2006. It was isolated from a soil-dwelling Gram-positive bacteria Bacillus cereus, along with another enzyme AlkC. AlkC and AlkD are most probably derived from the same protein as indicated by their close resemblance. They are also found in other prokaryotes. Among eukaryotes, they are found only in the single-celled species only, such as Entamoeba histolytica and Dictyostelium discoideum. The enzyme specifically targets 7mG (methyl-guanine) in the DNA, and is, therefore, unique among DNA glycosylases. It can also act on other methylpurines with less affinity. It indicates that the enzyme is specific for locating and cutting (excision) of chemically modified bases from DNA, exactly at 7mG, whenever there are errors in replication. It accelerates the rate of 7mG hydrolysis 100-fold over the spontaneous depurination. Thus, it protects the genome from harmful changes induced by chemical and environmental agents. Its crystal structure was described in 2008. It is the first HEAT repeat protein identified to interact with nucleic acids or to contain enzymatic activity.".
- Q21400335 abstract "AlkD (Alkylpurine glycosylase D) is an enzyme belonging to a family of DNA glycosylases that are involved in DNA repair. It was discovered by a team of Norwegian biologists from Oslo in 2006. It was isolated from a soil-dwelling Gram-positive bacteria Bacillus cereus, along with another enzyme AlkC. AlkC and AlkD are most probably derived from the same protein as indicated by their close resemblance. They are also found in other prokaryotes. Among eukaryotes, they are found only in the single-celled species only, such as Entamoeba histolytica and Dictyostelium discoideum. The enzyme specifically targets 7mG (methyl-guanine) in the DNA, and is, therefore, unique among DNA glycosylases. It can also act on other methylpurines with less affinity. It indicates that the enzyme is specific for locating and cutting (excision) of chemically modified bases from DNA, exactly at 7mG, whenever there are errors in replication. It accelerates the rate of 7mG hydrolysis 100-fold over the spontaneous depurination. Thus, it protects the genome from harmful changes induced by chemical and environmental agents. Its crystal structure was described in 2008. It is the first HEAT repeat protein identified to interact with nucleic acids or to contain enzymatic activity.".