Computational protein design enables a novel one-carbon assimilation pathway
Computational protein design enables a novel one-carbon assimilation pathway
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Author / Creator
Siegel, Justin B. , Lee Smith, Amanda , Poust, Sean , Wargacki, Adam J. , Bar-Even, Arren , Louw, Catherine , Shen, Betty W. , Eiben, Christopher B. , Tran, Huu M. , Noor, Elad , Gallaher, Jasmine L. , Bale, Jacob , Yoshikuni, Yasuo , Gelb, Michael H. , Keasling, Jay D. , Stoddard, Barry L. , Lidstrom, Mary E. and Baker, David
Publisher
United States: National Academy of Sciences
Journal title
Language
English
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Publisher
United States: National Academy of Sciences
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Scope and Contents
Contents
We describe a computationally designed enzyme, formolase (FLS), which catalyzes the carboligation of three one-carbon formaldehyde molecules into one three-carbon dihydroxyacetone molecule. The existence of FLS enables the design of a new carbon fixation pathway, the formolase pathway, consisting of a small number of thermodynamically favorable che...
Alternative Titles
Full title
Computational protein design enables a novel one-carbon assimilation pathway
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Record Identifier
TN_cdi_pubmed_primary_25775555
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_25775555
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1500545112
