Biochemistry · 2008 · 29 citations · 10 references
Life SciencesBiochemistryMolecular BiologyEnzymologyMetabolismMicrobial MetabolismCatalytic MechanismsMicrobial BiocatalysisMicrobial Sulfur CyclingSulfur ChemistrySulfur CycleSulfur MetabolismIsomerization CatalysisIsomerization ReactionsProton Transfer ReactionsRibulose-1, 5-Bisphosphate CarboxylationRubisco ActivityRubisco CarboxylationRubisco CatalysisSalvage
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.
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Structure-based activity prediction for an enzyme of unknown function
Johannes C. Hermann, Ricardo Martí‐Arbona, E.V. Fedorov et al. · Nature · 2007 · 258 citations · Full text
Thomas E. Hanson, F. Robert Tabita · Proceedings of the National Academy of Sciences · 2001 · 209 citations · Full text
Life Sciences, Biology, Microbiology +14
A Functional Link Between RuBisCO-like Protein of <i>Bacillus</i> and Photosynthetic RuBisCO
Hiroki Ashida, Y. SAITO, Chojiro Kojima et al. · Science · 2003 · 178 citations