Characterisation of Archaeglobus fulgidus AlkA hypoxanthine DNA glycosylase activity

FEBS Letters

Mansfield, Colin¹  McCarthy, Tommie V¹  Kerins, Sinéad M¹ 

[1] Department of Biochemistry, University College, Cork, Ireland

关键词: AlkA protein;    Hypoxanthine;    DNA glycosylase;    DNA repair;    Archaeglobus fulgidus;   

DOI  :  10.1016/S0014-5793(03)00257-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The AlkA protein from the archaebacterium Archaeglobus fulgidus was characterised with respect to release of hypoxanthine from DNA. The hypoxanthine glycosylase activity had optimal activity at 60°C at pH 5.0. The enzyme released hypoxanthine from substrates with a preference for dI:dG≫dI:dT>dI:dC>dI:dA. The presence of a mismatch on either side of the dIMP in the substrate reduced excision efficiency of the hypoxanthine residue at neutral pH, while a mismatch on both sides of the dIMP resulted in total loss of excision. Release of hypoxanthine from DNA required a minimum of two bases on the 5′ side and four bases on the 3′ side of the dIMP residue.

【 授权许可】

Unknown