Evolution of a designed retro-aldolase leads to complete active site remodeling

Nature Chemical Biology

Volumn 9, Issue 8, 2013, Pages 494-498

  Giger, Lars ^a   Caner, Sami ^a   Obexer, Richard ^a   Kast, Peter ^a   Baker, David ^b   Ban, Nenad ^a   Hilvert, Donald ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; LYSINE; SCHIFF BASE;

ARTICLE; CATALYSIS; COMPUTER MODEL; CONFORMATIONAL TRANSITION; DNA SHUFFLING; ENANTIOSELECTIVITY; ENZYME ACTIVE SITE; GLUCOSE METABOLISM; HYDROGEN BOND; HYDROPHOBICITY; MOLECULE; MUTAGENESIS; PRIORITY JOURNAL; PROTON TRANSPORT; SCREENING; STEREOCHEMISTRY; SUICIDE SUBSTRATE;

ALDEHYDE-LYASES; BIOCATALYSIS; CATALYTIC DOMAIN; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; DIRECTED MOLECULAR EVOLUTION; MODELS, MOLECULAR; MOLECULAR STRUCTURE;

EID: 84880920662     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1276     Document Type: Article

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