Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The pathways for catabolism of fructose were investigated in the type strains of Azospirillum lipoferum and Azospirillum brasilense grown aerobically with (NH4)2SO4 as the nitrogen source. When grown on fructose, the former species possessed a complete Entner-Doudoroff pathway, whereas the latter species lacked activity for glucose-6-phosphate dehydrogenase. Both species possessed a complete catabolic Embden-Meyerhof-Parnas pathway. Neither species possessed the key enzyme of the hexose monophosphate pathway, 6-phosphogluconate dehydrogenase. Both species could phosphorylate fructose to fructose-1-phosphate by means of a phosphoenolpyruvate-phosphotransferase system, and high activities of 1-phosphofructokinase occurred. Both species possessed glucokinase activity, but only A. lipoferum had hexokinase activity; moreover, the cells of A. brasilense were nearly impermeable to glucose, accounting for the inability of this species to grow on glucose. Both species possessed pyruvate dehydrogenase, a complete tricarboxylic acid cycle, a glyoxylate shunt, and malic enzyme. Analysis of the acidic end products for both species indicated the formation of only small amounts of various organic acids, and most of the titratable acidity was due to utilization of the ammonium ions of the medium. Gluconic acid was not formed during growth of either species on fructose but was detected during growth of A. lipoferum on glucose; this species also possessed an NADP-linked glucose dehydrogenase and gluconokinase.
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PMID:Fructose catabolism in Azospirillum brasilense and Azospirillum lipoferum. 673 86

Extracts containing uridine diphosphate (UDP) glucose dehydrogenase (EC 1.1.1.22) activity were prepared from rheumatoid and from normal human synovial cell lines using previously standardized techniques. Although no significant differences in the enzyme from the 2 sources were detected with respect to activity, substrate affinities, or responses to temperature and pH, these determinations have demonstrated that the enzyme is very sensitive to alterations in these parameters. The ultimate activity of the enzyme in vivo will be dependent upon the extent of the increased temperature, acidity, and altered glucose metabolism in the rheumatoid joint.
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PMID:Uridine diphosphate glucose dehydrogenase in rheumatoid synovial cells in culture. 731 Jul 71