@article{3227, keywords = {Escherichia coli, Mutagenesis, Computational Biology, Mutation, Kinetics, Dimerization, Escherichia coli Proteins, Protein Folding, Phenotype, Catalysis, Hydrolysis, Culture Media, Iron, Siderophores, Synthetic Biology, Enterobactin}, author = {Ann Donnelly and Grant Murphy and Katherine Digianantonio and Michael Hecht}, title = {A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli.}, abstract = {

Producing novel enzymes that are catalytically active in vitro and biologically functional in vivo is a key goal of synthetic biology. Here we describe Syn-F4, the first de novo protein that meets both criteria. Purified Syn-F4 hydrolyzes the siderophore ferric enterobactin, and expression of Syn-F4 allows an inviable strain of Escherichia coli to grow in iron-limited medium. These findings demonstrate that entirely new sequences can provide life-sustaining enzymatic functions in living organisms.

}, year = {2018}, journal = {Nat Chem Biol}, volume = {14}, pages = {253-255}, month = {2018 Mar}, issn = {1552-4469}, doi = {10.1038/nchembio.2550}, language = {eng}, }