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)

Bacterial strain PETP02(T) was isolated from nodules of Trifolium pratense growing in a Spanish soil. Phylogenetic analysis of the 16S rRNA gene sequence showed that this strain represents a member of the genus Phyllobacterium. However, divergence found with the 16S rRNA gene sequence of the single recognized species of this genus, Phyllobacterium myrsinacearum, indicated that strain PETP02(T) belongs to a different species. The results of DNA-DNA hybridization, phenotypic tests and fatty acid analyses confirmed that this strain represents a novel species of the genus Phyllobacterium, for which the name Phyllobacterium trifolii sp. nov. is proposed. The type strain is PETP02(T) (=LMG 22712(T)=CECT 7015(T)). This strain was strictly aerobic and used several carbohydrates as carbon source. It was not able to reduce nitrate. Aesculin hydrolysis was negative. It did not produce urease, arginine dihydrolase, gelatinase or beta-galactosidase. The DNA G+C content was 56.4 mol%. The nodD gene of this strain showed a sequence closely related to those of strains able to nodulate Lupinus. Infectivity tests showed that this strain is able to produce nodules in both Trifolium repens and Lupinus albus.
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PMID:Phyllobacterium trifolii sp. nov., nodulating Trifolium and Lupinus in Spanish soils. 1616 99

Two strains named ESC1(T) and ESC5 were isolated from nodules of Cytisus scoparius growing in a Spanish soil. Phylogenetic analysis of the 16S rRNA gene showed that these strains belong to the genus Ochrobactrum, their closest relatives being Ochrobactrum anthropi and Ochrobactrum lupini, with 100 and 99.9 % similarity to the respective type strains. Despite this high similarity, the results of DNA-DNA hybridization, phenotypic tests and fatty acid analyses showed that these strains represent a novel species of genus Ochrobactrum. The DNA-DNA hybridization values were respectively 70, 66 and 55 % with respect to O. lupini LUP21(T), O. anthropi DSM 6882(T) and Ochrobactrum tritici DSM 13340(T). The predominant fatty acids were C(18 : 1)omega7c and C(18 : 1) 2-OH. Strains ESC1(T) and ESC5 were strictly aerobic and were able to reduce nitrate and to hydrolyse aesculin. They produced beta-galactosidase and beta-glucosidase and did not produce urease after 48 h incubation. The G+C content of strain ESC1(T) was 56.4 mol%. Both strains ESC1(T) and ESC5 contained nodD and nifH genes on megaplasmids that were related phylogenetically to those of rhizobial strains nodulating Phaseolus, Leucaena, Trifolium and Lupinus. From the results of this work, we propose that the strains isolated in this study be included in a novel species named Ochrobactrum cytisi sp. nov. The type strain is ESC1(T) (=LMG 22713(T)=CECT 7172(T)).
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PMID:Ochrobactrum cytisi sp. nov., isolated from nodules of Cytisus scoparius in Spain. 1739 7

Because enzymes usually require distinct pH conditions for maximum activity, an approach of spontaneous pH shift of solution was devised to derive multiple reactions in a sequence. The two enzymes selected, horseradish peroxidase (HRP) and beta-galactosidase (GAL), had dissimilar optimal pH levels, i.e., 5.1 and 7.0, respectively. In a solution, HRP initially reacted at a lower pH range and the GAL reaction was consecutively carried out at a higher range in the presence of a third enzyme, urease, which caused an increase in pH. Under optimal conditions, the multiple system provided comparable performances with those of single reactions.
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PMID:Generation of colorimetric, dual signals from two different enzymes by using catalytic pH shift. 1862 23

A collection of 12 strains, isolated from diseased tortoises and tentatively identified as [Pasteurella] testudinis-like based on phenotypic characters, was compared with three reference strains of [P.] testudinis. All strains could be separated from the reference strains with respect to 16S rRNA gene sequences, partial sequences of the rpoB housekeeping gene and by phenotypic characters. Based upon differences in 16S rRNA and rpoB gene sequences, the new isolates are suggested to represent a novel species in a new genus of the family Pasteurellaceae Pohl 1981, for which the name Chelonobacter oris gen. nov., sp. nov. is proposed. The type strain is 1662(T) (=CCUG 55632(T)=DSM 21392(T)). beta-Haemolysis and acid production from (+)-l-arabinose, dulcitol, (-)-d-mannitol, (+)-d-mannose, trehalose and salicin separated the new strains from members of existing genera of the family Pasteurellaceae, in addition to the beta-galactosidase, urease and alpha-glucosidase reactions. Differences in indole production, phosphatase, beta-glucosidase and production of acid from dulcitol and trehalose separated C. oris from [P.] testudinis. Several phenotypic characters separated C. oris from Bisgaard's taxa 14 and 32.
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PMID:Comparative studies on [Pasteurella] testudinis and [P.] testudinis-like bacteria and proposal of Chelonobacter oris gen. nov., sp. nov. as a new member of the family Pasteurellaceae. 1957 48

Vibrio parahaemolyticus possessing urease-positive property is relatively rare, but such strains consistently exhibit the TDH-related hemolysin (TRH) gene. In this study, we examined the effects of incubation temperature on urease activity expression, using the TH3996 and AQ4673 strains where the enzyme activity is known to be temperature-dependent and -independent, respectively. In the TH3996 strain, beta-galactosidase activity was 4.4-fold lower after 30 degrees C cultivation than after 37 degrees in a ureR-lacZ fusion strain, but temperature dependency was not found in ureD- or nikA-lacZ fusion strains. However, ureR-, ureD-, and nikA-lacZ fusions of the AQ4673 strain was not influenced by incubation temperature. We compared the promoter sequences of ureR between the above two strains. Intriguingly, we detected mismatches of two nucleotides between the two strains located at positions -66 and -108 upstream of the methionine initiation codon for UreR. Additionally, urease activity was not affected by culture temperature at either 30 degrees or 37 degrees by allelic introduction of the AQ4673 ureR gene into the TH3996 ureR deletion mutant. Taken together, our study demonstrates that the transcriptional factor UreR is involved in the temperature dependency of urease activity, and two nucleotides within the ureR promoter region are of particular importance for the urease activity dependency of V. parahaemolyticus.
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PMID:Temperature-dependency urease activity in Vibrio parahaemolyticus is related to transcriptional activator UreR. 1999 1

The agar-degrading bacterium GNUM-1 was isolated from the brown algal species Sargassum serratifolium, which was obtained from the West Sea of Korea, by using the selective artificial seawater agar plate. The cells were Gram-negative, 0.5-0.6 micrometer wide and 2.0-2.5 micrometer long curved rods with a single polar flagellum, forming nonpigmented, circular, smooth colonies. Cells grew at 20 degrees C- 37 degrees C, between pH 5.0 and 9.0, and at 1-10% (w/v) NaCl. The DNA G+C content of the GNUM-1 strain was 45.5 mol%. The 16S rRNA sequence of the GNUM-1 was very similar to those of Alteromonas stellipolaris LMG 21861 (99.86% sequence homology) and Alteromonas addita R10SW13 T (99.64% sequence homology), which led us to assign it to the genus Alteromonas. It showed positive activities for agarase, amylase, gelatinase, alkaline phosphatase, esterase (C8), lipase (C14), leucine arylamidase, valine arylamidase, alpha-chymotrypsin, acid phosphatase, naphthol- AS-BI-phosphohydrolase, alpha-galactosidase, beta-galactosidase, beta-glucosidase, catalase, and urease. It can utilize citrate, malic acid, and trisodium citrate. The major fatty acids were summed feature 3 (21.5%, comprising C16:1omega7c/iso- C15:0 2-OH) and C16:0 (15.04%). On the basis of the variations in many biochemical characteristics, GNUM-1 was considered as unique and thus was named Alteromonas sp. GNUM-1. It produced the highest agarase activity in modified ASW medium containing 0.4% sucrose, but lower activity in rich media despite superior growth, implying that agarase production is tightly regulated and repressed in a rich nutrient condition. The 30 kDa protein with agarase activity was identified by zymography, and this report serves as the very first account of such a protein in the genus Alteromonas.
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PMID:Isolation and characterization of an agarase-producing bacterial strain, Alteromonas sp. GNUM-1, from the West Sea, Korea. 2322 23


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