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Glucose isomerase (also known as xylose isomerase) catalyzes the conversion of D-xylose and D-glucose to D-xylulose and D-fructose. Like most sugar isomerases, glucose isomerase catalyzes the interconversion of aldoses and ketoses. [24] The conversion of glucose to fructose is a key component of high-fructose corn syrup production.
Glucose-6-phosphate isomerase (GPI), alternatively known as phosphoglucose isomerase/phosphoglucoisomerase (PGI) or phosphohexose isomerase (PHI), is an enzyme ( EC 5.3.1.9) that in humans is encoded by the GPI gene on chromosome 19. [4] This gene encodes a member of the glucose phosphate isomerase protein family.
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 ).
Hepatocellular carcinoma (HCC [1]) is the most common type of primary liver cancer in adults and is currently the most common cause of death in people with cirrhosis. [2] HCC is the third leading cause of cancer-related deaths worldwide.
Triosephosphate isomerase deficiency is a rare autosomal recessive [2] metabolic disorder which was initially described in 1965. [ 3 ] It is a unique glycolytic enzymopathy that is characterized by chronic haemolytic anaemia , cardiomyopathy , susceptibility to infections, severe neurological dysfunction, and, in most cases, death in early ...
Triose phosphate isomerase is a highly efficient enzyme, performing the reaction billions of times faster than it would occur naturally in solution. The reaction is so efficient that it is said to be catalytically perfect : It is limited only by the rate the substrate can diffuse into and out of the enzyme's active site.
More recent studies link hepatitis C virus (HCV) infection to defects in fatty acid degradation, specifically, to that in enoyl-CoA isomerase. [23] HCV is the leading cause of chronic hepatitis, cirrhosis, and liver cancer, and more than 180 million people are affected globally. [24]