Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The levels of several enzymes have been studied during sporulation of Saccharomyces cerevisia. The specific activities of ribonuclease and aminopeptidase I raised several-fold after transfer of the cells to sporulation medium, whereas the specific activities of phosphofructokinase, glucose-6-phosphate dehydrogenase, tryptophan synthase and pyruvate decarboxylase were not significantly altered. The specific activities of NAD-dependent glutamate dehydrogenase, isocitrate lyase, malate dehydrogenase and fructose bisphosphatase all decreased from the onset of sporulation. The inactivation of these latter enzymes was inhibited by cycloheximide and by inhibitors of energy metabolism. Hexokinase, alcohol dehydrogenase and glutamate oxaloacetate transaminase were partially lost from the cells during the period of ascus maturation. None of the enzyme changes observed proved to be 'sporulation-specific' in that it occurred exclusively in sporulating diploid yeast cells. Therefore it is postulated that the meiotic events and the metabolic changes required for ascospore formation are under separate genetic control in this organism. During sporulation, the cellular content of cytochromes b, c, and aa3 was reduced to 20% or less of that present in vegetative derepressed cells. Since the relative percentage of total to cycloheximide-insensitive mitochondrial protein synthesis was not significantly altered throughout sporulation, and the pattern of mitochondrially synthesized polypeptides was rather similar both in vegetative and in sporulating cells, it appeared that not only degradation but also synthesis and therefore turnover of the mitochondrially coded polypeptides of cytochromes b and aa3 took place during sporulation. The activity ratio of cytochrome c oxidase to F1-ATPase in submitochondrial particles isolated from vegetative cells and from purified asci was almost identical. This indicates that the loss of membrane-bound mitochondrial cytochromes during sporulation is probably due to a nonselective degradation of inner mitochondrial membrane proteins.
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PMID:Protein degradation during yeast sporulation. Enzyme and cytochrome patterns. 18 44

The investigation of BDE-209 degradation by Microbacterium Y2 under different condition was conducted. Cell membrane permeability, cell surface hydrophobicity (CSH), membrane potential (MP) and reactive oxygen species (ROS) production were altered under BDE-209 stress. Eleven debrominated congeners were identified, suggesting that BDE-209 biodegradation by Microbacterium Y2 was dominantly a successive debromination process. Proteome analysis showed that the overexpression of haloacid dehalogenases, glutathione S-transferases (GSTs) and ATP-binding cassette (ABC) transporters might occupy important roles in BDE-209 biotransformation. Meanwhile, heat shock proteins (HSPs), ribonuclease E, oligoribonuclease (Orn) and ribosomal protein were activated to counter the BDE-209 toxicity. The up-regulated pyruvate dehydrogenase E1 component beta subunit and dihydrolipoamide dehydrogenase suggested that the pyruvate metabolism pathway was activated. Bioaugmentation of BDE-209 polluted water-sediments system with Microbacterium Y2 could efficiently improve BDE-209 removal. The detection of total 16S rRNA genes in treatment system suggested that Microbacterium (25.6 %), Luteimonas (14.3 %), Methylovorus (12.6 %), Hyphomicrobium (9.2 %) were the dominant genera and PICRUSt results further revealed that the diminution of BDE-209 was owed to cooperation between the introduced bacteria and aboriginal ones.
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PMID:Proteomic mechanism of decabromodiphenyl ether (BDE-209) biodegradation by Microbacterium Y2 and its potential in remediation of BDE-209 contaminated water-sediment system. 3180 41