Study of the role of the highly conserved residues Arg9 and Arg64 in the catalytic function of human N-acetyltransferases NAT1 and NAT2 by site-directed mutagenesis

Biochemical Journal

Volumn 323, Issue 1, 1997, Pages 207-215

  Deloménie, Claudine ^a   Goodfellow, Geoffrey H ^b   Krishnamoorthy, Rajagopal ^a   Grant, Denis M ^b   Dupret, Jean Marie ^a,c  

^a HÔPITAL ROBERT DEBRÉ   (France)

^b HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE   (Canada)

^c UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ALANINE; ARGININE; AROMATIC AMINE; CYSTEINE; GLUTAMINE; HYDROXYLAMINE; LYSINE; METHIONINE; RECOMBINANT ENZYME; XENOBIOTIC AGENT;

ARTICLE; BIOTRANSFORMATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STABILITY; ESCHERICHIA COLI; EXPRESSION VECTOR; GENETIC CONSERVATION; HUMAN; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ARGININE; ARYLAMINE N-ACETYLTRANSFERASE; CONSERVED SEQUENCE; CYSTINE; ENZYME STABILITY; HUMANS; HYDROGEN-ION CONCENTRATION; ISOENZYMES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHENYLGLYOXAL; PROTEIN DENATURATION; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030957457     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3230207     Document Type: Article

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