Glyceraldehyde-3-phosphate in glycolysis

TPI, another glycolytic enzyme that catalyzes the interconversion of dihydroxy-acetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate in glycolysis, was also oxidatively modified [32, 63, 66]. However, no change of TPI activity was observed [66], probably because the carbonyl groups added were localized away from the catalytic site of this enzyme. TPI was strongly inhibited by endogenous... 

Mn-SOD is an important antioxidant enzyme for the cell due to its role in detoxifying the free radical species superoxide (Oj), so HNE modification of this protein makes the cell more vulnerable to free radical attack. Alpha enolase facilitates the penultimate step of glycolysis by catalyzing the conversion of 2-phosphoglycerate into phosphoenolpyruvate. With HNE modification of alpha enolase, the cell is at risk of inadequate ATP stores due to inhibited production of pyruvate for fueling the citric acid cycle. Similarly, HNE modification of ATPase can lead to inhibited ATP formation due to the direct role of this enzyme in ATP synthesis. Triose phosphate isomerase catalyzes the reversible conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate in glycolysis and MDH catalyzes the oxidation of malate to oxaloacetate, so HNE modification of these proteins can also lead to lower ATP production. 

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See also in sourсe #XX -- [ , ]

See also in sourсe #XX -- [ ]

See also in sourсe #XX -- [ ]

See also in sourсe #XX -- [ , , , , , , ]

See also in sourсe #XX -- [ , ]

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