Ribose-5-phosphate isomerase  (Synonyms: Phosphoriboisomerase)

Ribose-5-phosphate isomerase (Phosphoriboisomerase) exists widely in microorganisms, animals and plants. It is the first enzyme in the non-oxidative phase of the pentose phosphate pathway (PPP) and also a key enzyme in the Calvin cycle (photosynthetic carbon fixation). Ribose-5-phosphate isomerase catalyzes the reversible isomerization between D-ribulose-5-phosphate (Ru5P) and D-ribose-5-phosphate (R5P). Ribose-5-phosphate isomerase acts as a multifunctional biocatalyst for rare sugar production. Ribose-5-phosphate isomerase serves as a target for antitrypanosomal agents^[1][2].

Ribose-5-phosphate isomerase can be used for the bioproduction of rare sugars, including D-Allose (HY-128741), L-Lyxose, L-Tagatose (HY-W145570) and L-Rhamnulose^[1].
Ribose-5-phosphate isomerase exists in two completely evolutionarily independent types. Among them, the Rpi of trypanosomes and Leishmania belongs to type B, while human hosts only have type A. The active sites of the two types differ significantly, allowing the design of selective RpiB inhibitors^[1].
Ribose-5-phosphate isomerase and transketolase colocalize in the chloroplast stroma of leaves from Pisum sativum var Little Marvel, suggesting a potential substrate channeling of ribose-5-P between the two enzymes^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9023-83-0

[Ribose-5-phosphate isomerase]

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• [1]. Chen J, et al. Ribose-5-phosphate isomerases: characteristics, structural features, and applications. Appl Microbiol Biotechnol. 2020;104(15):6429-6441.

  [2]. Anderson LE, et al. Enzyme co-localization with transketolase, xylulose-5-P 3-epimerase and phosphoriboisomerase in pea leaf chloroplasts. Plant Science. 2006 Dec 1;171(6):686-98.