Mutating a Highly Conserved Residue in Diverse Cytochrome P450s Facilitates Diastereoselective Olefin Cyclopropanation

ChemBioChem

Volumn 17, Issue 5, 2016, Pages 394-397

  Gober, Joshua G ^a   Rydeen, Amy E ^a   Gibson O'Grady, Evan J ^a   Leuthaeuser, Janelle B ^c   Fetrow, Jacquelyn S ^d   Brustad, Eric M ^a,b  

^a University of North Carolina at Chapel Hill   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

^c WAKE FOREST SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF RICHMOND   (United States)

Author keywords

biocatalysis; cyclopropanation; cytochromes; protein engineering

Indexed keywords

ALANINE; ALKENE; CYCLOPROPANE; CYTOCHROME P450; DIAZOACETIC ACID ETHYL ESTER; MOLECULAR SCAFFOLD; STYRENE; THREONINE; CYCLOPROPANE DERIVATIVE;

ARTICLE; BIOCATALYST; CYCLOPROPANATION; DIASTEREOISOMER; ENANTIOSELECTIVITY; GENE MUTATION; GENETIC VARIABILITY; PRIORITY JOURNAL; STEREOCHEMISTRY; CHEMISTRY; CONSERVED SEQUENCE; ENZYME ACTIVE SITE; GENETICS; MUTATION; STEREOISOMERISM;

ALKENES; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CYCLOPROPANES; CYTOCHROME P-450 ENZYME SYSTEM; MUTATION; STEREOISOMERISM;

EID: 84959431926     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201500624     Document Type: Article

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