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Volumn 40, Issue 45, 2001, Pages 13617-13622
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Mutation at active site lysine 212 to arginine uncouples the glycosylase activity from the lyase activity of human endonuclease III
a,b
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Author keywords
[No Author keywords available]
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Indexed keywords
SCHIFFS BASE;
AMINO ACIDS;
CHEMICAL BONDS;
DNA;
MASS SPECTROMETRY;
MUTAGENESIS;
ENZYMES;
AMINO ACID;
ARGININE;
DNA GLYCOSYLTRANSFERASE;
ENDONUCLEASE;
ENDONUCLEASE III;
GLYCINE;
GUANIDINE DERIVATIVE;
LYASE;
LYSINE;
SCHIFF BASE;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BETA SHEET;
CHEMICAL BOND;
COMPLEX FORMATION;
DNA ADDUCT;
ENZYME ACTIVITY;
HUMAN;
HYDROLYSIS;
MASS SPECTROMETRY;
POINT MUTATION;
PRIORITY JOURNAL;
PROTEIN DNA BINDING;
REACTION ANALYSIS;
REDUCTION;
SEQUENCE ANALYSIS;
SITE DIRECTED MUTAGENESIS;
AMINO ACID SUBSTITUTION;
ARGININE;
BINDING SITES;
CROSS-LINKING REAGENTS;
DEOXYRIBONUCLEASE (PYRIMIDINE DIMER);
DNA GLYCOSYLASES;
ENDODEOXYRIBONUCLEASES;
ESCHERICHIA COLI PROTEINS;
GENE DELETION;
HUMANS;
LYASES;
LYSINE;
MUTAGENESIS, SITE-DIRECTED;
N-GLYCOSYL HYDROLASES;
RECOMBINANT PROTEINS;
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EID: 0035856547
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011053b Document Type: Article |
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Times cited : (19)
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References (33)
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