Arginine 52 and histidine 54 located in a conserved amino-terminal hydrophobic region (LX2-R52-G-H54-X3-V-L) are important amino acids for the functional and structural integrity of the human liver UDP- glucuronosyltransferase UGT1*6

Molecular Pharmacology

Volumn 51, Issue 3, 1997, Pages 406-413

  Senay, Claire ^a,d   Ouzzine, Mohamed ^a,e   Battaglia, Eric ^a,c   Pless, Dorothy ^a   Cano, Virginie ^a   Burchell, Brian ^b   Radominska, Anna ^c   Magdalou, Jacques ^a,d   Fournel Gigleux, Sylvie ^a,d  

^a Centre du Medicament URA CNRS 597   (France)

^b UNIVERSITY OF DUNDEE   (United Kingdom)

^c UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

^d CNRS   (France)

^e UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

2,3 BUTANEDIONE; ARGININE; DIETHYL PYROCARBONATE; GLUCURONOSYLTRANSFERASE; HISTIDINE;

AMINO TERMINAL SEQUENCE; ARTICLE; ENZYME MODIFICATION; ENZYME STRUCTURE; GLUCURONIDATION; HUMAN; HUMAN CELL; HUMAN TISSUE; HYDROPHOBICITY; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ANIMALS; ARGININE; CELL LINE; CONSENSUS SEQUENCE; CRICETINAE; CRICETULUS; GLUCURONATES; GLUCURONOSYLTRANSFERASE; HISTIDINE; HUMANS; HYMECROMONE; LIVER; MUTAGENESIS, SITE-DIRECTED;

EID: 0030889553     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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