Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis

ACS Chemical Biology

Volumn 9, Issue 12, 2014, Pages 2843-2851

  Yachnin, Brahm J ^a,d   McEvoy, Michelle B ^a,d   Maccuish, Roderick J D ^a   Morley, Krista L ^c   Lau, Peter C K ^b,e   Berghuis, Albert M ^a,b,d  

^a Departments of Biochemistry   (Canada)

^b MCGILL UNIVERSITY   (Canada)

^c NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^d Groupes de Recherche GRASP et PROTEO   (Canada)

^e FQRNT Centre in Green Chemistry and Catalysis   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXANONE; ENZYME; LACTONE; MICROBIAL ENZYME; POLYCAPROLACTONE; UNSPECIFIC MONOOXYGENASE; BACTERIAL PROTEIN; CAPROLACTONE; CYCLOHEXANONE OXYGENASE; HEXANOIC ACID DERIVATIVE; OXYGENASE; PROTEIN BINDING;

ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME STRUCTURE; OXIDATION; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; STEREOCHEMISTRY; STEREOSPECIFICITY; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENE EXPRESSION; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MUTATION; PROTEIN ENGINEERING; RHODOCOCCUS; STEREOISOMERISM; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; BINDING SITES; BIOCATALYSIS; CAPROATES; CRYSTALLOGRAPHY, X-RAY; GENE EXPRESSION; LACTONES; MODELS, MOLECULAR; MUTATION; OXYGENASES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RHODOCOCCUS; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

EID: 84919668855     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500442e     Document Type: Article

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