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Global substitution of hemeproteins with noncanonical amino acids in Escherichia coli with intact cofactor maturation machinery
Citation key 164.2017.Völler
Author Völler, J.-S., and To, T., and Biava, H., and Koksch, B. and Budisa, N.
Pages 55 - 59
Year 2017
DOI https://doi.org/10.1016/j.enzmictec.2017.06.014
Journal Enzyme Microb. Technol.
Volume 106
Abstract Global substitution of canonical amino acids (cAAs) with noncanonical (ncAAs) counterparts in proteins whose function is dependent on post-translational events such as cofactor binding is still a methodically challenging and difficult task as ncAA insertion generally interferes with the cofactor biosynthesis machinery. Here, we report a technology for the expression of fully substituted and functionally active cofactor-containing hemeproteins. The maturation process which yields an intact cofactor is timely separated from cAA→ncAA substitutions. This is achieved by an optimised expression and fermentation procedure which includes pre-induction of the heme cofactor biosynthesis followed by an incorporation experiment at multiple positions in the protein sequence. This simple strategy can be potentially applied for engineering of other cofactor-containing enzymes.
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