Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.3.11 (glutamate dehydrogenase)
 4,437 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Wild-type Aspergillus nidulans grew equally well on NH4Cl, KNO3 or glutamine as the only nitrogen source. NADP+-dependent glutamate dehydrogenase (EC 1.4.1.4) and glutamine synthetase (GS; EC 6.3.1.2) activities varied with the type and concentration of nitrogen source supplied. Glutamate synthase (GOGAT) activity (EC 1.4.7.1) was detected but it was almost unaffected by the type and concentration of nitrogen source supplied. Ion exchange chromatography showed that the GOGAT activity was due to a distinct enzyme. Azaserine, an inhibitor of the GOGAT reaction, reduced the glutamate pool by 60%, indicating that GOGAT is involved in ammonia assimilation by metabolizing the glutamine formed by GS.
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PMID:The involvement of glutamine synthetase/glutamate synthase in ammonia assimilation by Aspergillus nidulans. 288 38

Glutamine is the first major organic product of assimilation of (13)NH(4) (+) by tobacco (Nicotiana tabacum L. cv. Xanthi) cells cultured on nitrate, urea, or ammonium succinate as the sole source of nitrogen, and of (13)NO(3) (-) by tobacco cells cultured on nitrate. The percentage of organic (13)N in glutamate, and subsequently, alanine, increases with increasing periods of assimilation. (13)NO(3) (-), used for the first time in a study of assimilation of nitrogen, was purified by new preparative techniques. During pulse-chase experiments, there is a decrease in the percentage of (13)N in glutamine, and a concomitant increase in the percentage of (13)N in glutamate and alanine. Methionine sulfoximine inhibits the incorporation of (13)N from (13)NH(4) (+) into glutamine more extensively than it inhibits the incorporation of (13)N into glutamate, with cells grown on any of the three sources of nitrogen. Azaserine inhibits glutamate synthesis extensively when (13)NH(4) (+) is fed to cells cultured on nitrate. These results indicate that the major route for assimilation of (13)NH(4) (+) is the glutamine synthetase-glutamate synthase pathway, and that glutamate dehydrogenase also plays a role, but a minor one. Methionine sulfoximine inhibits the incorporation of (13)N from (13)NO(3) (-) into glutamate more strongly than it inhibits the incorporation of (13)N into glutamine, suggesting that the assimilation of (13)NH(4) (+) derived from (13)NO(3) (-) may be mediated solely by the glutamine synthetase-glutamate synthase pathway.
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PMID:Initial organic products of assimilation of [N]ammonium and [N]nitrate by tobacco cells cultured on different sources of nitrogen. 1666 May 6