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A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis.

Nature chemical biology (2012-10-09)
Tobias J Erb, Bradley S Evans, Kyuil Cho, Benjamin P Warlick, Jaya Sriram, B McKay Wood, Heidi J Imker, Jonathan V Sweedler, F Robert Tabita, John A Gerlt
ABSTRACT

Functional assignment of uncharacterized proteins is a challenge in the era of large-scale genome sequencing. Here, we combine in extracto NMR, proteomics and transcriptomics with a newly developed (knock-out) metabolomics platform to determine a potential physiological role for a ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Rhodospirillum rubrum. Our studies unraveled an unexpected link in bacterial central carbon metabolism between S-adenosylmethionine-dependent polyamine metabolism and isoprenoid biosynthesis and also provide an alternative approach to assign enzyme function at the organismic level.

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Sigma-Aldrich
5′-Deoxy-5′-(methylthio)adenosine