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Ribulose is a ketopentose — a monosaccharide containing five carbon atoms, and including a ketone functional group. It has chemical formula C 5 H 10 O 5 . Two enantiomers are possible, d -ribulose ( d -erythro-pentulose) and l -ribulose ( l -erythro-pentulose).
Ribulose 1,5-bisphosphate (RuBP) is an organic substance that is involved in photosynthesis, notably as the principal CO 2 acceptor in plants. [ 1 ] : 2 It is a colourless anion, a double phosphate ester of the ketopentose ( ketone -containing sugar with five carbon atoms) called ribulose .
Ribulose 5-phosphate can be acted upon by phosphopentose isomerase to form ribose 5-phosphate, which is a precursor for nucleotide and co-factor biosynthesis. [1]
RuBisCO is important biologically because it catalyzes the primary chemical reaction by which inorganic carbon enters the biosphere.While many autotrophic bacteria and archaea fix carbon via the reductive acetyl CoA pathway, the 3-hydroxypropionate cycle, or the reverse Krebs cycle, these pathways are relatively small contributors to global carbon fixation compared to that catalyzed by RuBisCO.
Ribose 5-phosphate (R5P) is both a product and an intermediate of the pentose phosphate pathway.The last step of the oxidative reactions in the pentose phosphate pathway is the production of ribulose 5-phosphate.
Ribose-5-phosphate isomerase (Rpi) encoded by the RPIA gene is an enzyme (EC 5.3.1.6) that catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). It is a member of a larger class of isomerases which catalyze the interconversion of chemical isomers (in this case structural isomers of pentose).
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L-Ribulose 5-phosphate 4-epimerase catalyzes the epimerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate by retro-aldol cleavage and subsequent aldol reaction.The proposed mechanism involves the abstraction of the proton from the hydroxyl group on C-4, followed by cleavage of the bond between C-3 and C-4 to give a metal-stabilized acetone enediolate and a glycolaldehyde phosphate ...
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