Mechanistic diversity in the RuBisCO superfamily: A novel isomerization reaction catalyzed by the RuBisCO-like protein from Rhodospirillum rubrum

Heidi J Imker, Jaya Singh, Benjamin P. Warlick, F. Robert Tabita, John Alan Gerlt

Research output: Contribution to journalArticle

Abstract

Some homologues of D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) do not catalyze carboxylation and are designated RuBisCO-like proteins (RLPs). The RLP from Rhodospirillum rubrum (gi: 83593333) catalyzes a novel isomerization reaction (over-all 1,3-proton transfer reaction; likely, two 1,2-proton transfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate. Disruption of the gene encoding the RLP abolishes the ability of R. rubrum to utilize 5′-methylthioadenosine as a sole sulfur source, implicating a new, as-yet-uncharacterized, pathway for sulfur salvage.

Original languageEnglish (US)
Pages (from-to)11171-11173
Number of pages3
JournalBiochemistry
Volume47
Issue number43
DOIs
StatePublished - Oct 28 2008

ASJC Scopus subject areas

  • Biochemistry

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