Mutagenesis identifies the critical amino acid residues of human endonuclease G involved in catalysis, magnesium coordination, and substrate specificity

Journal of Biomedical Science

Volumn 16, Issue 1, 2009, Pages

  Wu, Shih Lu ^a   Li, Chia Cheng ^a   Chen, Jaw Chyun ^a   Chen, Yi Jin ^a   Lin, Ching Ting ^a   Ho, Tin Yun ^a   Hsiang, Chien Yun ^a  

^a CHINA MEDICAL UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; DIETHYL PYROCARBONATE; ENDONUCLEASE G; HISTIDINE; MAGNESIUM; AMINO ACID; DEOXYRIBONUCLEASE; HYDROXYLAMINE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; ENZYME SPECIFICITY; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN MOTIF; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; ANIMAL; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HELA CELL; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT;

ANABAENA; ESCHERICHIA COLI;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; CATALYSIS; ENDODEOXYRIBONUCLEASES; HELA CELLS; HUMANS; HYDROXYLAMINE; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 63449119852     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1186/1423-0127-16-6     Document Type: Article

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