Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: Evidence for the conservation of a cysteine protease catalytic domain and an active-site loop

Biochemical Journal

Volumn 356, Issue 2, 2001, Pages 327-334

  Rodrigues Lima, F ^a   Delomenie C ^a   Goodfellow, G H ^a   Grant, D M ^a   Dupret, J M ^a  

^a PITIÉ SALPÊTRIÈRE HOSPITAL   (France)

Author keywords

Acetyl CoA; Flexibility; Steric hindrance; Structure prediction; Substrate specificity

Indexed keywords

AMINES; CATALYSIS; CRYSTAL STRUCTURE; DETOXIFICATION; METABOLITES; STRUCTURAL ANALYSIS;

METABOLIC ACTIVATION;

ENZYMES;

ACETYL COENZYME A; ARYLAMINE ACETYLTRANSFERASE; ASPARTIC ACID; CYSTEINE; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; HISTIDINE; HYDRALAZINE; XENOBIOTIC AGENT;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BIOTRANSFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DETOXIFICATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; HUMAN; HUMAN CELL; HYDROXYLATION; METABOLIC ACTIVATION; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SALMONELLA TYPHIMURIUM; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; STEREOSPECIFICITY;

ACETYLTRANSFERASES; AMINO ACID SEQUENCE; ARYLAMINE N-ACETYLTRANSFERASE; CATALYTIC DOMAIN; CONSERVED SEQUENCE; HUMANS; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SALMONELLA TYPHIMURIUM; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0035365879     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3560327     Document Type: Article

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