How many and which amino acids are responsible for the large activity differences between the highly homologous UDP-glucuronosyltransferases (UGT) 1A9 and UGT1A10?

Drug Metabolism and Disposition

Volumn 38, Issue 4, 2010, Pages 687-696

  Itäaho, Katriina ^a   Laakkonen, Liisa ^a   Finel, Moshe ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

1 NAPHTHOL; AMINO ACID; CHIMERIC PROTEIN; DOBUTAMINE; ESTRADIOL; GLUCURONOSYLTRANSFERASE 1A10; GLUCURONOSYLTRANSFERASE 1A9; PROPRANOLOL;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; GLUCURONIDATION; POINT MUTATION; PRIORITY JOURNAL; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STEREOCHEMISTRY;

ADRENERGIC BETA-AGONISTS; ADRENERGIC BETA-ANTAGONISTS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO ACIDS; CATALYTIC DOMAIN; DOBUTAMINE; ESTRADIOL; GLUCURONIDES; GLUCURONOSYLTRANSFERASE; HUMANS; INDICATORS AND REAGENTS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NAPHTHOLS; PROPRANOLOL; SUBSTRATE SPECIFICITY;

HUMAN ECHOVIRUS 1;

EID: 77950270954     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.109.031229     Document Type: Article

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