Reductive dehydroxylation of allyl alcohols by IspH protein

Graewert T, Span I, Bacher A, Groll M (2010)


Publication Type: Journal article, Review article

Publication year: 2010

Journal

Book Volume: 49

Pages Range: 8802-8809

Journal Issue: 47

DOI: 10.1002/anie.201000833

Abstract

The way forward: In the last two decades a novel biosynthetic route to isopentenyl diphosphate and dimethylallyl diphosphate, the non-mevalonate or deoxyxylulose pathway, has been elucidated. The IspH protein (see space-filling model) catalyzes the terminal step of this biosynthetic pathway. The enzymes of this pathway are absent in mammals and are validated targets for new antibiotics. © 2010 WILEY-VCH Verlag GmbH & Co. KGaA.

Authors with CRIS profile

Involved external institutions

How to cite

APA:

Graewert, T., Span, I., Bacher, A., & Groll, M. (2010). Reductive dehydroxylation of allyl alcohols by IspH protein. Angewandte Chemie International Edition, 49(47), 8802-8809. https://dx.doi.org/10.1002/anie.201000833

MLA:

Graewert, Tobias, et al. "Reductive dehydroxylation of allyl alcohols by IspH protein." Angewandte Chemie International Edition 49.47 (2010): 8802-8809.

BibTeX: Download