Disease relevance of PGLS

• The protein was expressed in Escherichia coli, purified and shown to be 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway [1].
• Hemolytic anemia occurred in an individual who had inherited both the gene for 6-phosphogluconolactonase deficiency and that for deficiency of a nonhemolytic variant of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) [2].
• Computer simulation of the human erythrocyte hexose monophosphate shunt was used to investigate whether the severity of hemolysis, caused by deficiency of glucose-6-phosphate dehydrogenase, could be influenced by an accompanying deficiency of 6-phosphogluconolactonase [3].

High impact information on PGLS

• We studied the effect of glutathionylation on some of the enzymes identified in the present study and found that some of them (enolase and 6-phosphogluconolactonase) are inhibited by glutathionylation, whereas the enzymatic activity of cyclophilin (peptidylprolyl isomerase) is not [4].
• Partial deficiency of 6-phosphogluconolactonase (EC 3.1.1.31) of the erythrocytes was discovered as an autosomal dominant disorder [2].
• 6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency [2].
• Therefore, 6-phosphogluconolactonase activity accelerates hydrolysis of the delta form, thus preventing its conversion into the gamma form [5].
• NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase [5].

Biological context of PGLS

• The known kinetics of the enzymes involved in the oxidative part of the hexose monophosphate shunt suggest that partial deficiency of 6-phosphogluconolactonase would not restrict the rate of reduced nicotinamide-adenine dinucleotide phosphate production significantly [3].

Associations of PGLS with chemical compounds

• 6-Phosphogluconolactonase is the second enzyme of the oxidative branch and catalyzes the hydrolysis of 6-phosphogluconolactones, the products of glucose 6-phosphate oxidation by glucose-6-phosphate dehydrogenase [5].
• A spectrophotometric assay for 6-phosphogluconolactonase involving the use of immobilized enzymes to prepare the labile 6-phosphoglucono-delta-lactone substrate [6].
• These studies suggest that 6-phosphogluconolactonase is required for the functioning of the hexose monophosphate pathway when the rate of oxidation of NADPH is accelerated [7].
• In the absence of a reduced nicotinamide-adenine dinucleotide phosphate (NADPH)-oxidizing system, such as oxidized glutathione (GSSG)-glutathione reductase or phenazine methosulfate, little CO2 was formed, and the presence of 6-phosphogluconolactonase did not affect the amount that was produced [7].

References