Tetrahydrolipstatin inhibition, functional analyses, and three-dimensional structure of a lipase essential for mycobacterial viability

Journal of Biological Chemistry

Volumn 285, Issue 39, 2010, Pages 30050-30060

  Crellin, Paul K ^a   Vivian, Julian P ^a   Scoble, Judith ^a   Chow, Frances M ^b   West, Nicholas P ^b,c   Brammananth, Rajini ^a   Proellocks, Nicholas I ^a   Shahine, Adam ^a   Le Nours, Jerome ^a   Wilce, Matthew C J ^a   Britton, Warwick J ^b,c   Coppel, Ross L ^a   Rossjohn, Jamie ^a   Beddoe, Travis ^a  

^a MONASH UNIVERSITY   (Australia)

^b CENTENARY INSTITUTE   (Australia)

^c UNIVERSITY OF SYDNEY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; LIPASES; PROTEINS;

ARABINOGALACTAN; BIOSYNTHETIC PATHWAY; CATALYTIC TRIAD; CORE STRUCTURE; CORYNEBACTERIUM GLUTAMICUM; ENZYMATIC ASSAY; HOST CELLS; HYDROLASES; LIPASE ACTIVITY; M. TUBERCULOSIS; MYCOBACTERIAL; MYCOBACTERIAL CELLS; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; MYCOLIC ACIDS; OBESITY DRUGS; RECOMBINANT PROTEIN; THREE-DIMENSIONAL STRUCTURE;

CRYSTAL STRUCTURE;

ARABINOGALACTAN; HYDROLASE; MYCOLIC ACID; RECOMBINANT PROTEIN; TETRAHYDROLIPSTATIN; TRIACYLGLYCEROL LIPASE; BACTERIAL PROTEIN; ENZYME INHIBITOR; LACTONE;

ARTICLE; BACTERIAL CELL WALL; BACTERIAL VIABILITY; BIOSYNTHESIS; CONTROLLED STUDY; CORYNEBACTERIUM GLUTAMICUM; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME STRUCTURE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ANALYSIS; ANTAGONISTS AND INHIBITORS; CELL WALL; CHEMISTRY; ENZYMOLOGY; METABOLISM; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

CORYNEBACTERINEAE; CORYNEBACTERIUM GLUTAMICUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

BACTERIAL PROTEINS; CELL WALL; CORYNEBACTERIUM GLUTAMICUM; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; LACTONES; LIPASE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, TERTIARY;

EID: 77956944807     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.150094     Document Type: Article

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