Title : Mutation of a unique aspartate residue abolishes the catalytic activity but not substrate binding of the mouse N-methylpurine-DNA glycosylase (MPG).

Pub. Date : 2000 Feb 11

PMID : 10660595






2 Functional Relationships(s)
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1 Although Asp was identified as the active site residue in various DNA glycosylases based on the crystal structure, Glu-125 in human MPG (Glu-145 in mouse MPG) was recently proposed to be the catalytic residue. Glutamic Acid N-methylpurine DNA glycosylase Homo sapiens
2 Although Asp was identified as the active site residue in various DNA glycosylases based on the crystal structure, Glu-125 in human MPG (Glu-145 in mouse MPG) was recently proposed to be the catalytic residue. Glutamic Acid N-methylpurine DNA glycosylase Homo sapiens