The molecular recognition of streptomycin by Bacillus subtilis aminoglycoside-6-adenyl transferase has been analysed by a combination of NMR techniques and molecular dynamic simulations. This protein inactivates streptomycin by transferring an adenyl group to position six of the streptidine moiety. Our combined approach provides valuable information about the bioactive conformation for both the antibiotic and ATP and shows that the molecular recognition process for streptomycin involves a conformational selection phenomenon. The binding epitope for both ligands has also been analysed by 1D-STD experiments. Finally, the specificity of the recognition process with respect to the aminoglycoside and to the nucleotide has been studied.

The use of streptidine as a "decoy acceptor" allows the antibiotic activity of streptomycin to recover against the Escherichia coli strain overexpressing the aminoglycoside-modifying enzyme 6-O-adenyl transferase.

ANT(6) has a narrow tolerance to chemical variations in the aminoglycoside/nucleotide, making it very useful in the design of non-inactivable derivatives.

Three is not a crowd: Coexpression of the chaperonins GroEL/GroES with the α‐1,6‐fucosyltransferase from Rhizobium sp. allows a 10‐fold increase in production of soluble and active fucosyltransferase. The His‐tagged fucosyltransferase can be purified and immobilized on Ni2+‐IDA‐agarose gel in only one step (see Scheme). The immobilization leads to an important stabilization of the recombinant enzyme, which allows the preparation of a robust biocatalyst for the synthesis of oligosaccharides.