Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

At least three gluconic acid forming enzymes were identified in cell-free extracts of Aspergillus niger: glucose oxidase (EC 1.1.3.4), a glucose dehydrogenase (EC 1.1.99.10), and an enzyme or a mixture of enzymes catalyzing the cleavage of 6-phosphogluconate into gluconate and inorganic phosphate. 2,6-dichlorphenolindophenol was one of the hydrogen acceptors in vitro of the glucose dehydrogenase. Some properties of this enzyme (Km values, pH-dependence, substrate and hydrogen acceptor specificity), as determined in cell-free extracts, were found to be in good agreement with properties described in literature for a glucose dehydrogenase which has been purified from Aspergillus oryzae. The formation of Pi from 6-phosphogluconate and other phosphate esters was found to have an optimum between pH 7 and 8 , and another below pH 4. This suggests that it is catalyzed by an alkaline and an acid phosphomonoesterase (EC 3.1.3.1, 3.1.3.2), both enzymes exhibiting only low substrate specificity. The influence of extraction and assay buffers on the activity of gluconate forming enzymes was investigated. Loss of activity during preparation of cell-free extracts, as calculated from loss of activity storage of cell-free extracts at 4 degrees C, was found to be lower than 4%. Purified glucose oxidase added before homogenization was found in the extract almost quantitatively.
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PMID:[Gluconic acid forming enzymes in Aspergillus niger (author's transl)]. 1 16

The activities of alkaline and acid phosphatases, glucose dehydrogenase and NADH oxidase were assayed in cell-free extracts of sporogenic and asporogenic mutants of Clostridium botulinum. During growth of both mutants, the activities of alkaline and acid phosphatases were relatively constant, but during sporulation of the sporogenic mutant, the alkaline phosphatase activity rose to a maximum of 70 mumol/min x mg protein whereas the acid phosphatase decreased rapidly before it increased, indicating a possible role in sporogenesis. Glucose dehydrogenase activity was detected only in cell-free extracts of the sporogenic mutant and reached a maximum of 7 mumol/min x mg protein during the endospore maturation stage. The NADH oxidase activity was detected in both mutants. The NADH oxidase seems to stimulate glucose oxidation in both mutants during growth and the dehydrogenation processes of the butyric type of fermentation during spore formation in the sporogenic mutant. The findings suggest that increased glucose dehydrogenase activity in C. botulinum, as in Bacillus species, may serve as a spore event marker and that alkaline and acid phosphatases may play a regulatory role in anaerobic sporulation metabolism.
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PMID:Activity of some enzymes during growth and sporulation of Clostridium botulinum type E. 39 19

L-Malate repressed sporulation in the wild-type strain of Bacillus subtilis. When 75 mM L-malate was added to the growth medium at the time of inoculation, the appearance of heat-resistant spores was delayed 6 to 8 h. The synthesis of extracellular serine protease, alkaline phosphatase, glucose dehydrogenase, and dipicolinic acid was similarly delayed. Sporulation was not repressed when malate was added to the culture at t4 or later. A mutant was selected for ability to sporulate in the presence of malate. This strain could also sporulate in the presence of glucose. The malate-resistant mutant grew poorly with malate as sole carbon source, although it possessed an intact citric acid cycle, and it showed increased levels of malic enzyme. This indicates a defect in the metabolism of malate in the mutant. A mutant lacking malate dehydrogenase activity was also able to sporulate in the presence of malate. A model for the regulation of sporulation by malate is presented and discussed. Citric acid cycle intermediates other than malate did not affect sporulation. In contrast to previous results, sporulation of certain citric acid cycle mutants could be greatly increased or completely restored by the addition of intermediates after the enzymatic block. The results indicate that the failure of citric acid cycle mutants to sporulate can be adequately explained by lack of energy and lack of glutamate.
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PMID:Repression of sporulation in Bacillus subtilis by L-malate. 81 66

Netropsin, a polypeptide antibiotic which binds specifically to adenylate-thymidylate-rich regions of deoxyribonucleic acid, inhibitis sporulation at about stage II, but does not inhibit growth of Bacillys subtilis. An analysis of the sporulation-associated enzymes aconitase, alkaline phosphatase, and glucose dehydrogenase revealed that their rates of expression were not affected by the presence of the antibiotic. The derepression of histidase, a vegetatively induced enzyme was stimulated by netropsin. Oxygen utilization by the cells during sporulation was not effected nor was spore germination prevented by the drug. Netropsin, however, did prevent the formation of dipicolinic acid. These and earlier results suggest that netropsin may be affecting the transcription of only select sporulation genes that are particularly rich in adenylate-thymidylate base pairs.
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PMID:Effect of netropsin on the derepression of enzymes during growth and sporulation of Bacillus subtilis. 82 80

This report summarizes a one year evaluation of Abbott's ABA 100, with respect to mechanical parts (syringe plates, precision and linearity of photometry, band width of several filters, multicuvet precision, temperature control) and the reliability of several methods (endpoint procedures: determination of the glucose concentration with hexokinase- and the glucose dehydrogenase method, and of the protein concentration; enzyme activities: alanine and aspartate aminotransferase, creatine kinase, alkaline phosphatase). The critical batch size was estimated as an indicator of economy (about 40 samples per day for the glucose concentration). Various aspects of the instrument are discussed with respect to its use in clinical chemistry.
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PMID:Evaluation of the Abbott Bichromatic Analyzer 100 (A proposal for an evaluation scheme). 95 29

A transposon Tn917 insertion between gerE and ilvB has identified a new developmental locus, gerM, in Bacillus subtilis. gerM96::Tn917 affects both sporulation and germination. DNA on either side of the transposon has been cloned and includes the previously cloned sdhC and gerE loci. gerE terminates 2.1 kb from the end of the transposon. The gerM96::Tn917 mutant is oligosporogenous, yielding approximately 1% of the number of wild-type heat resistant spores in liquid medium and 10% on solid medium. Six hours after the onset of sporulation alkaline phosphatase and glucose dehydrogenase levels were 90% and 7%, respectively, of those of the wild-type. At this time 50% of the mutant cells were still dividing. The occurrence of multiple polar septa and 'pygmy' cells suggested a block at stage II of sporulation. Following addition of germinants, mutant spores prepared on nutrient agar lost heat resistance normally but released slightly less dipicolinic acid than wild-type spores. They also showed only partial loss of optical density, associated with a phase-grey appearance and striations in the cortex suggesting partial degradation. Expression of the gerM gene was monitored by production of beta-galactosidase encoded by a promotorless lacZ gene fused to the gerM96::Tn917 insertion. It occurred 1.5-4 h after commencement of sporulation. Transcription was directed from a promoter on the gerE side of gerM and was unaffected by a mutation in the gerE gene.
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PMID:Genetical and molecular studies on gerM, a new developmental locus of Bacillus subtilis. 284 48

Batch cultures of Aspergillus niger grown from conidia on a medium with high C/N ratio accumulated gluconate from glucose with a yield of 57%. During almost the whole time of accumulation there was no net synthesis of total protein in the mycelium but the activity per flask and the specific activity of glucose oxidase (EC 1.1.3.4) in mycelial extracts increased whereas both values decreased for glucose dehydrogenase (EC 1.1.99.10) 'gluconate 6-phosphatase' (cf. EC 3.1.3.1, 3.1.3.2), gluconokinase (EC 2.7.1.12), glucose 6-phosphate and phosphogluconate dehydrogenases (EC 1.1.1.49, EC 1.1.1.44), phosphoglucomutase (EC 2.7.5.1), and most enzymes of the Embden-Meyerhof pathway and the tricarboxylic acid cycle. Gluconate dehydratase (EC 4.2.1.39), gluconate dehydrogenase (EC 1.1.99.3) and enzymes of the Entner-Doudoroff pathway could not be detected. By cycloheximide the increase of glucose oxidase activity was inhibited. It is concluded that the high yield of gluconate was due mainly to the net (de novo) synthesis of glucose oxidase which occurred during protein turnover after the exhaustion of the nitrogen source, and which was not accompanied by a net synthesis of the other enzymes investigated. Some gluconate may also have been formed by hydrolytic cleavage of gluconate 6-phosphate.
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PMID:Gluconate accumulation and enzyme activities with extremely nitrogen-limited surface cultures of Aspergillus niger. 301 15

A comparison was made of morphological changes and successive, mainly biochemical, marker events for sporulation in 14 asporogenous mutants. The morphological and biochemical sequences are linked so that arrested development in one is accompanied by corresponding effects in the other. Thus mutants that fail to produce both protease and antibiotic do not progress beyond stage 0, formation of alkaline phosphatase appears to be associated with the transition from stage II to stage III and glucose dehydrogenase with that from stage III to stage IV. Stage II mutants may produce ;pygmy' cells or other bizarre cell-division forms. The biochemical sequence is dependent in the sense that if the occurrence of any one event is blocked that of all the succeeding events is also blocked. This has implications for biochemical models that have been proposed to explain the temporal sequence observed in spore development.
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PMID:Sporulation in Bacillus subtilis. Correlation of biochemical events with morphological changes in asporogenous mutants. 499 77

The activity of endocellular enzymes (alkaline phosphatase, protease, glucose dehydrogenase, aldolase, malate dehydrogenase, NADH dehydrogenase, NADH oxidase) was studied in isolated prospores and sporangia as well as in vegetative cells of Bacillus thuringiensis strains, one of which produced crystals and one did not. The activity of malate dehydrogenase and NADH dehydrogenase was high in prospores of the both strains at the fifth and sixth stages of spore formation. The strain which did not produce crystals differed from the parent strain by a higher aldolase activity at all of the growth stages and by an abrupt increase in the activity of hydrolytic enzymes in sporangia (in the cytoplasm of the parent cells).
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PMID:[Activity of intracellular enzymes in Bacillus thuringiensis prospores and sporangia]. 634 86

Three sporulation mutants have been isolated which produce spores with an atypical resistance phenotype, i.e. they are sensitive to organic solvents and heat but resistant to lysozyme. All three mutants produced serine protease, alkaline phosphatase and glucose dehydrogenase which are biochemical marker events for stages I, II and III. Two of the three mutants produced dipicolinic acid, a late marker, but the third was defective in its production. Heat-resistance was not restored to any of the mutants by the provision of exogenous dipicolinate. Gel electrophoresis showed that the mutant spores had similar patterns of spore coat proteins to the wild-type and electron microscopy revealed no significant structural differences. The three mutations responsible for the phenotypes of the mutant spores lie in the phe-argA region of the Bacillus subtilis chromosome. Recombination index values indicate that the mutations are in three separate genes. They define at least two new sporulation loci, designated spoVH and spoVJ.
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PMID:SpoVH and spoVJ--new sporulation loci in Bacillus subtilis 168. 640 8


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