Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597: Discovery of a deacylating water molecule and insight into enzyme inactivation

Journal of Molecular Biology

Volumn 400, Issue 4, 2010, Pages 743-754

  Mileni, Mauro ^a   Kamtekar, Satwik ^b   Wood, David C ^b   Benson, Timothy E ^b   Cravatt, Benjamin F ^a   Stevens, Raymond C ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b PFIZER GLOBAL RESEARCH AND DEVELOPMENT   (United States)

Author keywords

Catalytic mechanism; Crystal structure; Deacylating water; Fatty acid amide hydrolase (FAAH); URB597

Indexed keywords

AMIDASE; CHYMOTRYPSIN; CYCLOHEXYLCARBAMIC ACID 3' CARBAMOYLBIPHENYL 3 YL ESTER; ELASTASE; FATTY ACID AMIDASE; SERINE PROTEINASE; TRYPSIN; WATER;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DEACYLATION; ENZYME INACTIVATION; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN INTERACTION;

EID: 77954385220     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.05.034     Document Type: Article

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