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Ribose-5-phosphate isomerase deficiency (RPID) is a rare human disorder caused by mutations in ribose-5-phosphate isomerase, an enzyme of the pentose phosphate pathway.With only four known cases – all diagnosed between 1984 and 2019 – RPI deficiency is the second rarest disease, with Fields condition being the rarest, affecting two known individuals, Catherine and Kirstie Fields.
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 ).
Crystal structure of ribose 5-phosphate isomerase and ribose 5-phosphate complex in E. coli. R5P consists of a five-carbon sugar, ribose, and a phosphate group at the five-position carbon. It can exist in open chain form or in furanose form. The furanose form is most commonly referred to as ribose 5-phosphoric acid. [1]
The pentose phosphate pathway. The pentose phosphate pathway (also called the phosphogluconate pathway and the hexose monophosphate shunt or HMP shunt) is a metabolic pathway parallel to glycolysis. [1] It generates NADPH and pentoses (five-carbon sugars) as well as ribose 5-phosphate, a precursor for the synthesis of nucleotides. [1]
In enzymology, a ribose isomerase (EC 5.3.1.20) is an enzyme that catalyzes the chemical reaction D-ribose ⇌ {\displaystyle \rightleftharpoons } D-ribulose Hence, this enzyme has one substrate , D-ribose , and one product , D-ribulose .
Phosphohexose Isomerase Deficiency (PHI) is also known as phosphoglucose isomerase deficiency or Glucose-6-phosphate isomerase deficiency, and is a hereditary enzyme deficiency. PHI is the second most frequent erthoenzyopathy in glycolysis besides pyruvate kinase deficiency , and is associated with non-spherocytic haemolytic anaemia of variable ...
With four diagnosed patients in 27 years, [needs update?] ribose-5-phosphate isomerase deficiency is considered the second rarest. [3] [4] While no single number has been agreed upon for which a disease is considered rare, several efforts have been undertaken to estimate the number of unique rare diseases.
The first published description of a structure of a prokaryotic phosphopentomutase was in 2011. [1] Structures of Bacillus cereus phosphopentomutase as it was purified, after activation, bound to ribose 5-phosphate and bound to glucose 1,6-bisphosphate are deposited in the PDB with accession codes 3M8W, 3M8Y, 3M8Z and 3OT9, respectively.