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)

Treatment of cell suspension cultures of Phaseolus vulgaris c.v. Immuna with an elicitor preparation heat-released from the cell walls of the phytopathogenic fungus Colletotrichum lindemuthianum resulted in rapid accumulation of the prenylated 5-hydroxyisoflavanone phytoalexin kievitone followed by later accumulation of the pterocarpan-derived phytoalexin phaseollin. Kievitone formation was preceded by rapid transient increases in the extractable activities of the enzymes L-phenylalanine ammonia-lyase and chalcone synthase. The extractable activities of 15 enzymes were measured in the cell cultures during the period of kievitone accumulation. The results suggest a highly selective induction of enzymes associated directly with the phytoalexin pathway. No induction of enzymes of pathways diverging from or providing substrates for the phenylpropanoid----isoflavonoid pathway was observed. The increase in glutamate dehydrogenase activity in control cultures was prevented by elicitor application. A comparison of enzyme activities in control and Colletotrichum-infected bean hypocotyls provided further evidence of the selective induction of enzymes of phytoalexin synthesis, although peroxidase, glutamate dehydrogenase and glutamate synthase activities were higher in infected than in healthy hypocotyls. It is concluded that the major enzymic changes occurring in elicitor-treated bean cells are probably those directly associated with defence mechanisms such as the formation of isoflavonoid phytoalexins (this paper) or accumulation of phenolic compounds and hydroxyproline-protein in the cell walls [Bolwell, G. P. et al. (1985) Eur. J. Biochem. 148, 571-578].
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PMID:Metabolic changes in elicitor-treated bean cells. Selectivity of enzyme induction in relation to phytoalexin accumulation. 399 94

Yeast mutants lacking proteinase A were isolated. One of these mutants (Hb I) is characterized in detail. The mutation called pra1 segregates 2:2 in meiotic tetrads indicating a single gene mutation. No anti-(proteinase A) cross-reacting material can be detected. Diploids heterozygous for pra1 show gene dosage. Thus, it appears that PRA1 might be the structural gene for proteinase A. Results obtained with this mutant show that proteinase A is not a vital component of the vegetative cell cycle. The mutant exhibits normal mitotic growth under rich and poor growth conditions and shows normal mating. Enzymes subject to carbon catabolite inactivation and inactivation of NADP-dependent glutamate dehydrogenase, processes which were proposed to be of proteolytic nature, are not affected by the absence of proteinase A. However, protein degradation under sporulation conditions is about 30% reduced in proteinase A mutant cells. The differentiation process of sporulation is also disturbed leading to a 40% reduced sporulation frequency in mutant cells.
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PMID:Analysis of proteinase A function in yeast. 679 92