Histidine-193 of rat glucosylceramide synthase resides in a UDP-glucose- and inhibitor (D-threo-1-phenyl-2-decanoylamino-3-morpholinopropan-1-ol)-binding region: A biochemical and mutational study

Biochemical Journal

Volumn 341, Issue 2, 1999, Pages 395-400

  Wu, Kangjian ^a   Marks, David L ^a   Watanabe, Rikio ^a   Paul, Pascal ^a,b   Rajan, Niveda ^a   Pagano, Richard E ^a  

^a MAYO CLINIC   (United States)

^b SANOFI   (France)

Author keywords

D threo 1 phenyl decanoylamino 3 morpholinopropan 1 ol; Diethyl pyrocarbonate; Glycosphingolipids; Glycosyltransferase; Golgi apparatus

Indexed keywords

1 PHENYL 2 DECANOYLAMINO 3 MORPHOLINOPROPAN 1 OL; BRAIN ENZYME; CERAMIDE; CERAMIDE GLUCOSYLTRANSFERASE; DIETHYL PYROCARBONATE; ENZYME INHIBITOR; GLUCOSE; GLUCOSYLCERAMIDE; GLYCOSPHINGOLIPID; HISTIDINE; HYDROXYLAMINE; MUTANT PROTEIN; SYNTHETASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME INHIBITION; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; ENZYME INHIBITORS; GLUCOSYLTRANSFERASES; HISTIDINE; HUMANS; MOLECULAR SEQUENCE DATA; MORPHOLINES; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; RATS; SEQUENCE ALIGNMENT; URIDINE DIPHOSPHATE GLUCOSE;

EID: 0033565926     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3410395     Document Type: Article

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