Mechanistic diversity in the RuBisCO superfamily: a novel isomerization reaction catalyzed by the RuBisCO-like protein from Rhodospirillum rubrum.
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 (overall 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.
Imker
Heidi J
HJ
Department of Microbiology and Plant Cellular and Molecular Biology Department/Plant Molecular Biology/Biotechnology Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210, USA.
Singh
Jaya
J
Warlick
Benjamin P
BP
Tabita
F Robert
FR
Gerlt
John A
JA
D002384:Catalysis; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D012247:Rhodospirillum rubrum / Q000235:genetics / Q000378:metabolism*; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D011506:Proteins; D012273:Ribulose-Bisphosphate Carboxylase