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

Journal of Biological Chemistry

Volumn 275, Issue 6, 2000, Pages 4278-4282

  Roy, Rabindra ^a   Biswas, Tapan ^a,b   Lee, J Ching ^a   Mitra, Sankar ^a  

^a UNIVERSITY OF TEXAS MEDICAL BRANCH   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA GLYCOSYLTRANSFERASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME SUBSTRATE COMPLEX; EXCISION REPAIR; MOUSE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ACID; BINDING SITES; CIRCULAR DICHROISM; DNA FOOTPRINTING; DNA GLYCOSYLASES; DNA REPAIR; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; N-GLYCOSYL HYDROLASES; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECTROMETRY, FLUORESCENCE;

EID: 0034635534     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.6.4278     Document Type: Article

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