| uracil-DNA glycosidase | <enzyme> Catalyses hydrolysis of n-glycosidic bond of damaged nucleotide residues to give free uracil and partly depyrimidinated DNA of unaltered chain length; does not cleave phosphodiester bonds; a DNA repair enzyme Registry number: EC 3.2.2.- Synonym: ura-DNA glycosidase, uracil-DNA glycosylase, uracil n-glycosidase, ura-DNA glycosylase, uracil n-glycosylase (26 Jun 1999) |
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| foldback DNA | <molecular biology> Sections of single-stranded DNA which have sequences that are palindromes, or which read the same both backwards and forwards, that may base pair with each other instead of with the right sections of the other strand during renaturation into double-stranded DNA. (09 Oct 1997) |
| 5-methylcytosine-DNA glycosylase | <enzyme> Binds equally well to methylated and non-methylated DNA; isolated from developing chicken embryos and mouse fibroblasts; mw 52.5 kD Registry number: EC 3.2.2.- (26 Jun 1999) |
| 8-hydroxy-5-deazaflavin-dependent DNA photolyase | <enzyme> From anacystis nidulans; purified in streptomyces coelicolor; distinguish from folate-dependent DNA photolyase Registry number: EC 4.1.99.- Synonym: 8-hdfd-DNA photolyase (26 Jun 1999) |
| formamidopyridine-DNA glycosylase | <enzyme> Substrate is the ring-opened form of 7-methylguanine; has been sequenced; genbank af026691 Registry number: EC 3.2.2.23 Synonym: fap-DNA glycosylase, fapy-DNA glycosylase, formamidopyrimidine-DNA glycosylase, 8-oxoguanine DNA glycosylase, 8-hydroxyguanine DNA glycosylase, 8-hydroxyguanine endonuclease, 8-oh-gua endonuclease, fpg protein, E coli, fpg gene product, E coli, mutm protein, oh8 guanine excision repair enzyme, ogg1 gene product (26 Jun 1999) |
| forms of DNA i, II and III | Refers to circular DNA removed from viruses and as plasmids. Form I is the DNA in its normal, supercoiled form. Form II is the DNA after one of the two strands has been nicked (cut apart), and is circular. Form III is the DNA after both strands have been broken, and is linear. (09 Oct 1997) |
| linker DNA | The DNA found between nucleosomes on chromatin; since it is not complexed to proteins as strongly as other forms of DNA, it is accessible to exonuclease hydrolysis. (05 Mar 2000) |