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

The effect of gossypol, a polyphenolic compound with antifertility action on human males, has been investigated on the following oxidoreductases purified from human tissues: lactate dehydrogenase (EC 1.1.1.27) isozymes 1 or B4 from heart, 5 or A4 from liver and X or C4 from spermatozoa; malate dehydrogenase (EC 1.1.1.37) mitochondrial and "soluble" isozymes from heart and NADP-glutamate dehydrogenase (EC 1.4.1.4) from liver. Gossypol proved to be a powerful inhibitor of the six enzymes studied. For all of them, inhibition was of the competitive type with respect to the coenzyme and non-competitive in relation to substrate. The lowest ki values were shown for lactate dehydrogenase isozyme 1 or B4 and for the two isozymes of malate dehydrogenase. Results did not show selectivity of gossypol for the sperm-specific isozyme X or C4 of lactate dehydrogenase.
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PMID:In vitro inhibition by gossypol of oxidoreductases from human tissues. 375 38

The effects of gossypol, a polyphenolic compound isolated from the cotton plant upon six oxidoreductases from cultured epimastigotes of Typanosoma cruzi were studied. Gossypol was a powerful inhibitor of the alpha-hydroxyacid and malate dehydrogenases, NAD-linked enzymes, and of glutamate dehydrogenase, malic enzyme and glucose-6-phosphate dehydrogenase, NADP-dependent enzymes. The drug did not have an effect on succinate dehydrogenase, a flavoprotein. The Ki values with respect to substrate were 0.73, 0.3 and 3.5 microM for alpha-hydroxyacid, malate and glutamate dehydrogenases, respectively, and 1.1, 0.19 and 7.8 microM with respect to the coenzyme. Inhibition was noncompetitive with respect to substrate and uncompetitive in relation to the coenzyme.
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PMID:Inhibition by gossypol of oxidoreductases from Trypanosoma cruzi. 637 Feb 65

Gossypol was isolated and purified from cotton seed flour. It was found to inhibit rat testis cytosolic LDH-X activity, in vitro, in a dose-dependent manner. Preincubation of the enzyme with gossypol increased the inhibitory effect markedly. Addition of NADH to the preincubation mixture imparted some protection against inhibition. The inhibitory effect of gossypol was competitive with respect to NADH, but non-competitive with respect to alpha-ketoglutarate. The latter is reported to be a specific substrate for rat LDH-X and hence can be used for measuring LDH-X activity in the presence of other lactic dehydrogenase isoenzymes. Preliminary studies show that gossypol can inhibit other dehydrogenases such as glutamic dehydrogenase, glutathione reductase and malic dehydrogenase as well.
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PMID:Inhibition of rat testis LDH-X activity by gossypol. 716 54