Aldose Reductase: Difference between revisions
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[[Aldose Reductase]] (AldR) is an NADPH-dependent enzyme which reduces aldehydes and carbonyls. It reduces glucose to sorbitol in the glucose metabolism pathway. The AldR is implicated in diabetics and causing Iodine Deficiency Disorder (IDD) and its treatment involves the use of IDD inhibitors of AldR. The images at the left and at the right correspond to one representative AldR, ''i.e.'' the crystal structure of barley apo-Aldose Reductase ([[2bgq]]). | [[Aldose Reductase]] (AldR) is an NADPH-dependent enzyme which reduces aldehydes and carbonyls. It reduces glucose to sorbitol in the glucose metabolism pathway. The AldR is implicated in diabetics and causing Iodine Deficiency Disorder (IDD) and its treatment involves the use of IDD inhibitors of AldR. The images at the left and at the right correspond to one representative AldR, ''i.e.'' the crystal structure of barley apo-Aldose Reductase ([[2bgq]]). | ||
'''Fructose bisphosphate aldolase''' is an enzyme in glycolysis and gluconeogenesis. Glycolyis is responsible for the conversion of glucose into two three-carbon pyruvate molecules without the need for oxygen. The process generates two net ATP. The overall reaction is: | |||
Glucose + 2 NAD+ + 2 ADP + 2 Pi --> 2 pyruvate (3-carbon product) + 2 NADH + 2 ATP + 2 H20 + 4 H+ | |||
Gluconeogenesis is responsible for maintaining the appropriate levels of blood glucose in animals by generating glucose from non-carbohydrate precursors. Gluconeogenesis can make glucose from lactate, pyruvate, citric acid cycle intermediates and from most amino acids (the exceptions being leucine and lysine). The common intermediate for all of the precursors on their way to becoming glucose must be oxaloacetate. | |||
The aldolase catalyzes the reversible cleavage of fructose-1,6-bisphosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP). Different isozymes of aldolase can also catalyze the cleavage of fructose 1-phosphate to diydroxyacetone and glyceraldehyde (GA). Different isozymes exhibit preferences for either or both of the substrates, depending on the role of the aldolase (i.e. gluconeogenesis versus glycolysis).<ref name="book">Voet, D, Voet, J, & Pratt, C. (2008). Fundamentals of biochemistry, third edition. Hoboken, NJ: Wiley & Sons, Inc.</ref> | |||
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