Journal Article

Biochemical evidence supporting the presence of the classical mevalonate pathway in the thermoacidophilic archaeon Sulfolobus solfataricus

Hiroto Nishimura, Yasuhiro Azami, Masahito Miyagawa, Chika Hashimoto, Tohru Yoshimura and Hisashi Hemmi

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 153, issue 5, pages 415-420
Published in print May 2013 | ISSN: 0021-924X
Published online February 2013 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/jb/mvt006
Biochemical evidence supporting the presence of the classical mevalonate pathway in the thermoacidophilic archaeon Sulfolobus solfataricus

Show Summary Details

Preview

The existence of the classical mevalonate (MVA) pathway was examined in the thermoacidophilic archaeon Sulfolobus solfataricus. The pathway is considered uncommon among archaea because the genes of the orthologues of phosphomevalonate kinase (PMK) and/or diphosphomevalonate decarboxylase (DMD) are absent in the genomes of most archaea. Instead, the modified MVA pathway, which involves isopentenyl phosphate kinase (IPK), has been proposed to exist in the archaea that lack the classical pathway. However, some archaea including S. solfataricus possess the genes of the orthologues of both IPK and all enzymes of the classical pathway. Biochemical characterization using recombinant proteins showed that the orthologues of the enzymes catalyzing the late steps of the classical pathway, i.e. MVA kinase, PMK and DMD, are all active. Moreover, in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from S. solfataricus indicated that only the classical pathway likely works in the organism.

Keywords: archaea; isoprenoid; mevalonate pathway; Sulfolobus

Journal Article.  4204 words.  Illustrated.

Subjects: Biochemistry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content. subscribe or login to access all content.