Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The objective of the present study was to characterize the metabolism of Clostridium thermolacticum, a thermophilic anaerobic bacterium, growing continuously on lactose (10 g l(-1)) and to determine the enzymes involved in the pathways leading to the formation of the fermentation products. Biomass and metabolites concentration were measured at steady-state for different dilution rates, from 0.013 to 0.19 h(-1). Acetate, ethanol, hydrogen and carbon dioxide were produced at all dilution rates, whereas lactate was detected only for dilution rates below 0.06 h(-1). The presence of several key enzymes involved in lactose metabolism, including beta-galactosidase, glyceraldehyde-3-phosphate dehydrogenase, pyruvate:ferredoxin oxidoreductase, acetate kinase, ethanol dehydrogenase and lactate dehydrogenase, was demonstrated. Finally, the intracellular level of NADH, NAD+, ATP and ADP was also measured for different dilution rates. The production of ethanol and lactate appeared to be linked with the re-oxidation of NADH produced during glycolysis, whereas hydrogen produced should come from reduced ferredoxin generated during pyruvate decarboxylation. To produce more hydrogen or more acetate from lactose, it thus appears that an efficient H2 removal system should be used, based on a physical (membrane) or a biological approach, respectively, by cultivating C. thermolacticum with efficient H2 scavenging and acetate producing microorganisms.
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PMID:Metabolism of lactose by Clostridium thermolacticum growing in continuous culture. 1650 46

Both apicomplexan parasites Toxoplasma gondii and Plasmodium falciparum lack type I NADH dehydrogenases (complex I) but instead carry alternative (type II) NADH dehydrogenases, which are absent in mammalian cells and are thus considered promising antimicrobial drug targets. The quinolone-like compound 1-hydroxy-2-dodecyl-4(1H)quinolone (HDQ) was recently described as a high-affinity inhibitor of fungal alternative NADH dehydrogenases in enzymatic assays, probably by interfering with the ubiquinol binding site of the enzyme. We describe here that HDQ effectively inhibits the replication rates of P. falciparum and T. gondii in tissue culture. The 50% inhibitory concentration (IC50) of HDQ for T. gondii was determined to be 2.4+/-0.3 nM with a growth assay based on vacuole sizes and 3.7+/-1.4 nM with a growth assay based on beta-galactosidase activity. Quantification of the P. falciparum replication rate using a fluorometric assay revealed an IC50 of 14.0+/-1.9 nM. An important feature of the HDQ structure is the length of the alkyl side chain at position 2. Derivatives with alkyl side chains of C6, C8, C12 (HDQ), and C14 all displayed excellent anti-T. gondii activity, while a C5 derivative completely failed to inhibit parasite replication. A combined treatment of T. gondii-infected cells with HDQ and the antimalarial agent atovaquone, which blocks the ubiquinol oxidation site of cytochrome b in complex III, resulted in synergism, with a calculated fractional inhibitory concentration of 0.16 nM. Interference of the mitochondrial ubiquinone/ubiquinol cycle at two different locations thus appears to be a highly effective strategy for inhibiting parasite replication. HDQ and its derivatives, particularly in combination with atovaquone, represent promising compounds with a high potential for antimalarial and antitoxoplasmal therapy.
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PMID:Growth inhibition of Toxoplasma gondii and Plasmodium falciparum by nanomolar concentrations of 1-hydroxy-2-dodecyl-4(1H)quinolone, a high-affinity inhibitor of alternative (type II) NADH dehydrogenases. 1724 51

The objective of this collaborative study was to determine the method performance characteristics of a spectrophotometric enzymatic assay for measuring the lactose content of fluid milk. The principle behind the method is similar to that of AOAC Method 984.15 but with significant modifications and added quality control. Additionally, lactose concentration is expressed on a weight/weight (wt/wt) rather than a weight/volume (wt/vol) basis. The principle of the method is the hydrolysis of lactose to D-glucose and D-galactose by beta-galactosidase, followed by the oxidation of beta-D-galactose by nicotinamide adenine dinucleotide (NAD+) in the presence of beta-galactose dehydrogenase. The reaction is catalyzed by the addition of aldose-l-epimerase, which accelerates the mutarotation of alphha-D-galactose to beta-D-galactose. The amount of reduced nicotinamide adenine dinucleotide (NADH) formed is measured at 340 nm and is proportional to the amount of lactose present. Important aspects of the assay include preparing the assay solution by weight (rather than volume), mixing the contents of the spectrophotometric cuvette without losing solution, inclusion of aldose-l-epimerase, specifying spectrophotometer characteristics, and accounting for the optical path length of the spectrophotometric cuvettes. In the collaborative study, 11 laboratories tested one lactose standard and 8 pairs of blind replicate raw, processed, and formulated milks with an anhydrous lactose content between 3.0-7.2%. Statistical performance, in units of g/100 g anhydrous lactose, for the milk materials within the applicability of the method was as follows: mean = 4.4040, Sr = 0.0130, SR = 0.0250, RSDr = 0.29%, RSDR = 0.57%, r = 0.0364, and R = 0.0700. Standard and marginal recoveries were 98.66 and 99.53%, respectively. Method performance represented a significant improvement over what would be achieved if path length was not accounted for or the assay was done volumetrically. The Study Directors recommend that the method for determination of the lactose content of fluid milk by the spectrophotometric enzymatic method using weight additions and path length adjustment be adopted Official First Action.
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PMID:Determination of the lactose content of fluid milk by spectrophotometric enzymatic analysis using weight additions and path length adjustment: collaborative study. 1737 52

The mitochondrial aspartate-glutamate carriers (AGC) aralar (SLC25A12) and citrin (SLC25A13) are components of the malate aspartate shuttle (MAS), a major intracellular pathway to transfer reducing equivalents from NADH to the mitochondrial matrix. Aralar is the main AGC isoform present in the adult brain, and it is expressed mainly in neurons. To search for the other AGC isoform, citrin, in brain glial cells, we used a citrin knockout mouse in which the lacZ gene was inserted into the citrin locus as reporter gene. In agreement with the low citrin levels known to be present in the adult mouse brain, beta-galactosidase expression was very low. Surprisingly, unlike the case with astroglial cultures that express citrin, no beta-galactosidase was found in brain glial cells. It was confined to neuronal cells within discrete neuronal clusters. Double-immunolabelling experiments showed that beta-galactosidase colocalized not with glial cell markers but with the pan-neuronal marker NeuN. The deep cerebellar nuclei and a few midbrain nuclei (reticular tegmental pontine nuclei; magnocellular red nuclei) were the regions where beta-galactosidase expression was highest, and it was up-regulated in fasted mice, as was also the case for liver beta-galactosidase. The results support the notion that glial cells have much lower AGC levels and MAS activity than neurons.
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PMID:Low levels of citrin (SLC25A13) expression in adult mouse brain restricted to neuronal clusters. 1990 84


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