Nature Chemical Biology 4, 715 (2008). doi:10.1038/nchembio1208-715

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Nature Chemical Biology 4, 718 (2008). doi:10.1038/nchembio1208-718

Author: Jeffrey T. Borenstein

Bacterial infections have long been associated with coagulation, but the mechanism is not well understood. New insights into bacterial spatial localization are shedding light on how bacterial clusters can trigger coagulation in a process known as 'quorum acting'.

Nature Chemical Biology 4, 719 (2008). doi:10.1038/nchembio1208-719

Authors: Marco W Fraaije & Andrea Mattevi

The berberine bridge enzyme catalyzes the crucial step in the biosynthesis of an important class of alkaloids through a reaction that cannot be carried out using conventional organic chemistry tools. Characterization of the enzyme demonstrates a concerted mechanism that couples two distinct chemical steps—oxidation and proton abstraction—affecting two separate groups of the substrate.

Nature Chemical Biology 4, 721 (2008). doi:10.1038/nchembio1208-721

Authors: Minoru Fukuda & Xingfeng Bao

Cell-surface carbohydrates are synthesized in a step-wise fashion, yielding products with unique capping structures. A recent study has shown that carbohydrates at the cell surface can be further remodeled by an endogenous glycosidase to alter the carbohydrate structure, thus generating a new function.

Nature Chemical Biology 4, 722 (2008). doi:10.1038/nchembio1208-722

Authors: Bing Qi & J Marie Hardwick

Small-molecule inhibitors of anti-apoptotic Bcl-2 proteins and BH3 mimetic peptides are promising anticancer agents. A recent study identifies a Nur77-based peptide that converts anti-apoptotic Bcl-2 proteins into pro-apoptotic molecules, providing another potential cancer therapeutic strategy.

Nature Chemical Biology 4, 723 (2008). doi:10.1038/nchembio1208-723

Author: Matthew D Disney

Isoginkgetin has been identified as a general inhibitor of pre-mRNA splicing using an in vivo screening assay. This and related inhibitors will not only be useful as tools to decipher the roles of the individual components of the spliceosome but may also serve as therapeutics.

Nature Chemical Biology 4, 725 (2008). doi:10.1038/nchembio1208-725

Author: David M J Lilley

X-ray scattering from clusters of gold atoms provides a sensitive way of measuring long-range distance information in macromolecules and now reveals a surprisingly soft, stretchy character to double-stranded DNA.

A concerted mechanism for berberine bridge enzyme

Nature Chemical Biology 4, 739 (2008). doi:10.1038/nchembio.123

Authors: Andreas Winkler, Andrzej Łyskowski, Sabrina Riedl, Martin Puhl, Toni M Kutchan, Peter Macheroux & Karl Gruber

Berberine bridge enzyme catalyzes the conversion of (S)-reticuline to (S)-scoulerine by formation of a carbon-carbon bond between the N-methyl group and the phenolic ring. We elucidated the structure of berberine bridge enzyme from Eschscholzia californica and determined the kinetic rates for three active site protein variants. Here we propose a catalytic mechanism combining base-catalyzed proton abstraction with concerted carbon-carbon coupling accompanied by hydride transfer from the N-methyl group to the N5 atom of the FAD cofactor.