Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.3.4.6 (urease)
 7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arginine is rapidly depleted from the medium during the cultivation of T. vaginalis in a defined or semi-defined medium. It is broken down to ornithine, ammonia and carbon dioxide by the three enzymes of the dihydrolase pathway: arginine deiminase, catabolic ornithine carbamyltransferase (OCTase) and carbamate kinase. Arginase and urease as well as citrulline hydrolase appear to be absent. Ornithine, a product of the pathway was further converted to putrescine by an active ornithine decarboxylase. Apparent substrate Km values determined were arginine deiminase, 103 microM; catabolic OCTase, 71 microM; ornithine decarboxylase 134 microM. A substrate level phosphorylation is associated with the pathway; the significance of this to the overall energy economy of the cell is unclear.
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PMID:The pathway of arginine catabolism in the parasitic flagellate Trichomonas vaginalis. 631 11

Parabens were found to be potent inhibitors of alkali production from arginine by oral streptococci such as Streptococcus rattus, Streptococcus sanguis and Streptococcus gordonii. For example, 2 mumol butylparaben per ml completely and irreversibly inhibited arginolysis by intact cells of S. rattus FA-1 and was lethal for the organism. In contrast, butylparaben was not a very effective inhibitor of ureolysis by intact cells of Streptococcus salivarius 57.I, although it did kill the cells. Butylparaben irreversibly inhibited the cytoplasmic enzymes arginine deiminase, carbamate kinase and urease in permeabilized cells or isolated form. However, inhibition of arginolysis by intact cells appeared to be due primarily to irreversible inhibition of transport systems for arginine uptake, because butylparaben added to intact cells did not reduce levels of arginine deiminase when the cells were subsequently permeabilized after washing. The insensitivity of ureolysis by intact cells to butylparaben can be related to the known high permeability of cell membranes to urea and the cytoplasmic location of urease. The potency of butylparaben as an inhibitior of arginolysis or glycolysis and as a lethal agent was found to be greater at acid pH that at neutral or alkaline pH.
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PMID:Membrane locus and pH sensitivity of paraben inhibition of alkali production by oral streptococci. 1055 Nov 69

Slackia exigua ATCC 700122(T) and Cryptobacterium curtum ATCC 700683(T) were our isolates from infected root canal and human periodontal pocket, respectively; they are asaccharolytic anaerobic gram-positive rods, which are predominant in the oral cavity. They utilize arginine, so our aim was to investigate the pathway of arginine degradation. Metabolic end products were determined with high-performance liquid chromatography. The related enzymatic activities in cell-free extract were also assayed. Both S. exigua and C. curtum degraded arginine and produced substantial amounts of citrulline, ornithine and ammonia. Arginine and citrulline supported the growth of both strains. As the related enzymatic activities, arginine deiminase, ornithine carbamoyltransferase and carbamate kinase activities were detected in the cell-free extract of S. exigua and C. curtum. Arginase and urease activities were not detected in either organism. These results suggest that arginine was metabolized by the arginine deiminase pathway. Both S. exigua and C. curtum degrade arginine via the arginine deiminase pathway.
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PMID:Degradation of arginine by Slackia exigua ATCC 700122 and Cryptobacterium curtum ATCC 700683. 1706 96