Peer-Reviewed Journal Details
Mandatory Fields
Mansfield C, Kerins SM, McCarthy TV;
2003
April
Febs Letters
Characterisation of Archaeglobus fulgidus AlkA hypoxanthine DNA glycosylase activity.
Validated
()
Optional Fields
540
1-3
171
175
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 degrees 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.
14-5793
http://www.sciencedirect.com/science/article/B6T36-485G79B-1/2/7c334a831133f58f8e6d128846551547
Grant Details