Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In parenchymal cells from starved mice L-tryptophan is a potent inhibitor of gluconeogenesis from substrates giving rise to oxaloacetate. Quinolinate yields a different pattern of inhibition and is generally much less effective. Tryptamine, indole 3-acetaldehyde and indole 3-acetate are equally as effective as tryptophan. Tryptamine inhibition alone may be overcome by pargyline; serotonin does not prevent the inhibition due to tryptophan. In kidney slices from starved rats, however, tryptophan has no effect on gluconeogenesis. Indole 3-acetate is also relatively ineffective, but quinolinate is signficiantly more potent than in liver; at 0.1mM, glucose production from lactate is 50% inhibited. Quinolinate is less effective with citric acid cycle substrates; the pattern of inhibition is consistent with a direct action on phosphoenolpyruvate carboxykinase. There is no evidence that glutamate dehydrogenase is simultaneously inhibited.
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PMID:Effect of tryptophan and its metabolites on gluconeogenesis in mammalian tissues. 124 97