The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads

Biochemical and Biophysical Research Communications

Volumn 389, Issue 2, 2009, Pages 247-250

  Nam, Ki Hyun ^a   Kim, Soo Jin ^b   Priyadarshi, Amit ^a   Kim, Hyun Sook ^a   Hwang, Kwang Yeon ^a  

^a Korea University   (South Korea)

^b National Academy of Agricultural Science   (South Korea)

Author keywords

Active site inhibition; Charge relay system; EstE5; EstE5 PMSF; Esterase lipase

Indexed keywords

BENZYLSULFONYL FLUORIDE; ESTE5 ENZYME; ESTERASE; ESTERASE INHIBITOR; HORMONE SENSITIVE LIPASE; NUCLEOPHILE; SERINE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME STRUCTURE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FUNCTION;

CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; PROTEASE INHIBITORS; PROTEIN CONFORMATION; SERINE; STEROL ESTERASE; TOSYL COMPOUNDS;

ANIMALIA; RODENTIA;

EID: 70349322388     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.08.123     Document Type: Article

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