Ribose-5-phosphate isomerase: Difference between revisions
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==Introduction== | ==Introduction== | ||
'''Ribose 5-phosphate isomerase''' (Rpi) is a highly conserved protein that acts as an enzyme in both eukaryotic and prokaryotic metabolic pathways<ref name="rpi">PMID:12517338</ref>. Specifically, Rpi catalyzes the reaction that converts <scene name='Sandbox_Reserved_305/Ligand/1'> ribose-5-phosphate </scene> (R5P) to ribulose-5-phosphate (Ru5P). Rpi exists as two distinct protein forms known as RpiA and RpiB, both of which catalyze the same reaction, and most organisms express one or both of these enzymes. | '''Ribose 5-phosphate isomerase''' (Rpi) is a highly conserved protein that acts as an enzyme in both eukaryotic and prokaryotic metabolic pathways<ref name="rpi">PMID:12517338</ref>. Specifically, Rpi catalyzes the reaction that converts <scene name='Sandbox_Reserved_305/Ligand/1'> ribose-5-phosphate </scene> (R5P) to ribulose-5-phosphate (Ru5P). Rpi exists as two distinct protein forms known as RpiA and RpiB, both of which catalyze the same reaction, and most organisms express one or both of these enzymes. | ||
The functional and structural properties of RpiA have been determined from organisms including ''Escherichia coli, Pyrococcus horikoshii, Saccharomyces cerevisiae,'' among others<ref name="rpi">PMID:12517338</ref>. These studies have revealed an important role RpiA plays in the [[Calvin cycle]] in plants and pentose phosphate pathway in both plants and animals <ref name="rpi2">PMID:19214439</ref>. The sequence conservation among RpiA subfamilies also shows the considerable evolutionary significance in preserving its function across different organisms. | The functional and structural properties of '''RpiA''' have been determined from organisms including ''Escherichia coli, Pyrococcus horikoshii, Saccharomyces cerevisiae,'' among others<ref name="rpi">PMID:12517338</ref>. These studies have revealed an important role RpiA plays in the [[Calvin cycle]] in plants and pentose phosphate pathway in both plants and animals <ref name="rpi2">PMID:19214439</ref>. The sequence conservation among RpiA subfamilies also shows the considerable evolutionary significance in preserving its function across different organisms. | ||
*'''RpiB''' does not exist in humans and is structurally unrelated to RplA<ref>PMID:27230471</ref>. | |||
==Function== | ==Function== | ||