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De Novo Protein Provides Life‐Sustaining Enzymatic Function in Auxotrophic E. coli
Author(s) -
Mularz Ann,
Smith Betsy,
Hecht Michael
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.720.3
Subject(s) - enterobactin , siderophore , auxotrophy , escherichia coli , ferric , enzyme , biochemistry , esterase , chemistry , ferric ion , microbiology and biotechnology , biology , gene , organic chemistry
Bacterial siderophores, which exhibit exceptionally high affinities for ferric iron, often require a specific enzyme to release the bound iron for subsequent use in cellular processes. E. coli produces the siderophore enterobactin, which is cleaved by the enzyme ferric enterobactin esterase (Fes). Without Fes, importing ferric enterobactin is futile, ultimately resulting in cell death from lack of bioavailable iron. Here, we report on the creation of a de novo siderophore‐cleaving enzyme, SynF4. The expression of SynF4 in auxotrophic Δ fes E. coli enables survival in iron deficient environments. Evolved from a library of de novo proteins, SynF4 is an esterase, cleaving the E. coli siderophore ferric enterobactin which allows iron to be released. This is the first example of a life‐enabling de novo enzyme. This research was funded by the National Defense Science and Engineering Graduate Fellowship of the Department of Defense and by grants MCB‐1050510 and MCB‐1409402 from the NSF.