A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism

Journal of Biological Chemistry

Volumn 285, Issue 29, 2010, Pages 22264-22275

  Dresen, Carola ^a   Lin, Leo Y C ^a   D'Angelo, Igor ^a   Tocheva, Elitza I ^a,b   Strynadka, Natalie ^a   Eltis, Lindsay D ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CATABOLIC GENES; CATABOLIC PATHWAY; CATALYTIC RESIDUE; DELETION MUTANTS; FLAVIN-DEPENDENT; FLAVIN-DEPENDENT MONOOXYGENASE; FUNCTIONAL DATAS; HYDROXYLASES; KETO GROUPS; MONOOXYGENASES; MYCOBACTERIUM TUBERCULOSIS; OXYGENASES; RHODOCOCCUS; RIGID BODY ROTATION; SECOND CRYSTAL; SUBSTRATE SPECIFICITY;

BINDING ENERGY; CHOLESTEROL; CONFORMATIONS; ENZYMES; METABOLISM; PHENOLS; ROTATION;

CRYSTAL STRUCTURE;

3 HYDROXY 9,10 SECONANDROST 1,3,5(10) TRIENE 9,17 DIONE; 3 HYDROXY 9,10 SECONANDROST 1,3,5(10) TRIENE 9,17 DIONE 4 HYDROXYLASE; 3,17 DIHYDROXY 9,10 SECONANDROST 1,3,5(10) TRIENE 9 ONE; 3,9 DIHYDROXY 9,10 SECONANDROST 1,3,5(10) TRIENE 9,17 ONE; 4 HYDROXYPHENYL ACETATE DEHYDROXYGENASE; ARGININE; CHOLESTEROL; QUERCETIN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; VALINE;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; LIPID DEGRADATION; MOLECULAR DOCKING; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL;

BACTERIAL PROTEINS; BINDING SITES; BIOCATALYSIS; CHOLESTEROL; CRYSTALLOGRAPHY, X-RAY; FLAVINS; GAS CHROMATOGRAPHY-MASS SPECTROMETRY; GENE DELETION; HYDROXYLATION; KINETICS; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PHENOTYPE; PROTEIN STRUCTURE, SECONDARY;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS; RHODOCOCCUS JOSTII;

EID: 77954575769     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.099028     Document Type: Article

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