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Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
Published on: August 19, 2013
3-Methyladenine-DNA glycosylase I from Escherichia coli-computer modeling and supporting experimental evidence
D Plochocka1, A Kierzek, T Obtulowicz
1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Abstract:
TagA (3-methyladenine-DNA glycosylase I) excises 3-methyadenine and 3-methylguanine from alkylated DNA. The structure of this enzyme has not yet been determined experimentally. We propose a three-dimensional model of the TagA protein based on the threading algorithm. The model shows that TagA is a mostly alpha-helical protein, in agreement with circular dichroism measurements. None of the eight cysteines present in the TagA sequence forms a disulfide bridge in the model structure, which has also been experimentally verified with the use of Ellman method.
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