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Background:The archaeon Thermococcus kodakarensis harbors an uncharacterized member of the ribokinase family encoded by TK2285. Results: The structure of the TK2285 protein was elucidated, and the protein exhibited unexpected kinase activity toward myo-inositol. Conclusion:The Thermococcales harbor a novel, archaea-type ribokinase family member with activity toward myo-inositol. Significance: Our results raise the possibility of a novel mechanism of inositol metabolism in Archaea.

We report progress in elucidating the structure of nisin, a naturally occurring peptide antibiotic. Nisin contains five rings constrained by lanthionine or methyllanthionine bridges, as well as alpha, beta-unsaturated amino acids. We have determined conformations for two model compounds of ring A and a derivative of ring B through interactive nmr and computer simulation studies. High-resolution nmr techniques provides structural information, which was further refined through molecular dynamics simulations. These methods are being applied to the remaining constrained fragments of the molecule. This conformational information will be employed in an aufbau approach to determining the structure of the entire molecule.

A crystalline salt of tryptamine with trans-3-nitrocinnamic acid underwent cross photocycloaddition, leading to a cyclobutane adduct 1. Their solid mixture failed to give 1. This is the first [2+2] photocycloaddition of alkene to “N-unsubstituted” indoles.