Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Treatment of 2-acetamido-2-deoxy-D-mannono-1,4-lactone with dicyclohexylamine in ethanolic solution afforded an unsaturated 1,4-lactone, 2-acetamido-2,3-dideoxy-D-erythro-hex-2-enono-1,4-lactone (1), in good yield. 2-Acetamido-2,3-dideoxy-D-threo-hex-2-enono-1,4-lactone (2) was similarly prepared from 2-acetamido-2-deoxy-D-galactono-1,4-lactone. An unsaturated 1,5-lactone, 2-acetamido-2,3-dideoxy-D-threo-hex-2-enono-1,5-lactone (4), was obtained through the oxidation of 2-acetamido-2-doexy-4,6-0-isopropylidene-D-galactopyranose with silver carbonate on Celite, followed by mild hydrolysis. The inhibitory activity of four isomeric 2-acetamido-2,3-dideoxy-D-hex-2-enonolactones [1, 2, 4, and 2-acetamido-2,3-dideoxy-D-erythro-hex-2-enono-1,5-lactone (3)] was assayed against 2-acetamido-2-deoxy-beta-D-glucosidase from bull epididymis. Only the erythro lactones 1 and 3 are weak competitive inhibitors, whereas the threo lactones 2 and 4 are practically inactive. The 1,4-lactone 1 inhibited 2-acetamido-2-deoxy-beta-D-glucosidase more strongly than the 1,5-lactone 3. The lactones 1-4 were found to be quite stable in aqueous solution or under inhibitory-assay conditions. In addition, two 2-acetamido-2-deoxy-D-glycals, 2-acetamido-1,5-anhydrohex-1-enitol (7) were tested; both are 10 times as active as 1.
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PMID:The inhibitory activities of 2-acetamido-2,3-dideoxy-D-hex-2-enonolactones on 2-acetamido-2-deoxy-beta-D-glucosidase. 123 69

The serum concentrations of FSH, LH, prolactin, testosterone, and estradiol and the enzymatic activities of hyaluronidase, glucosidases (alpha-glucosidase, beta-glucosidase, alpha-mannosidase, N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and beta-galactosidase), lactate dehydrogenase and its isoenzymes (LDH1, LDH2, LDH3, LDH-X, LDH4), and total proteins were measured in the semen of 69 subjects (8 normozoospermic controls, 7 secretory, and 54 excretory azoospermic subjects). FSH levels rose with the deterioration in spermatogenesis and served to differentiate the secretory from the excretory azoospermias. The only source of hyaluronidase and LDH-X in the ejaculate is the spermatozoa. alpha-Glucosidase activity essentially originates in the epididymis. The seminal determination of alpha-glucosidase and, to a lesser extent, alpha-mannosidase and N-acetyl-beta-D-glucosaminidase helps rapidly, sensitivity, reliably, and noninvasively to differentiate secretory azoospermias (with higher enzymatic activity) from the excretory type (less enzymatic activity) and may be of use in identifying with a certain degree of reliability the site of obstruction in the male genital tract.
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PMID:Enzyme and hormonal markers in the differential diagnosis of human azoospermia. 153 Mar 67

Rat spermatozoa were recovered from the caput, corpus, and cauda epididymides and assayed for glycosidase activity, total nonamino (neutral) carbohydrate, and protein content. The activities of beta-glucosidase, beta-galactosidase, beta-N-acetylglucosaminidase, and beta-N-acetylgalactosaminidase were fluorometrically assayed in spermatozoa and membrane-enriched fractions. Except for beta-glucosidase, the activities of the glycosidases based on protein content were greatest in whole sperm and membrane-enriched fractions obtained from the cauda epididymides. Based on sperm concentration, however, glycosidase activities increased proceeding from the caput to the corpus epididymides, then declined from the corpus to the cauda epididymides. Analyses of nonamino carbohydrate and protein content based on sperm number indicated regional trends similar to those of glycosidase activity. Total nonamino carbohydrate and protein content were highest in corpus sperm, and lowest in cauda sperm. These data indicate major quantitative changes in cell surface carbohydrate as spermatozoa traverse the epididymis. A positive correlation for the membrane-enriched fraction between increasing glycosidase activity and decreasing carbohydrate and protein content suggests that glycosidases may play a significant role in modifying the spermatozoon surface during epididymal transit and maturation.
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PMID:Changes in rat sperm membrane glycosidase activities and carbohydrate and protein contents associated with epididymal transit. 359 43

1. The previous study (Conchie, Gelman & Levvy, 1967b) of the specificity of beta-glucosidase, beta-galactosidase and beta-d-fucosidase in barley, limpet, almond emulsin and rat epididymis was extended to alpha-l-arabinosidase. 2. The inhibitory action of l-arabinono-(1-->5)-lactone was tested against all four types of enzyme, and alpha-l-arabinosidase was examined for inhibition by glucono-, galactono- and d-fucono-lactone. 3. In emulsin, the enzyme that hydrolyses beta-glucosides, beta-galactosides and beta-d-fucosides also hydrolyses alpha-l-arabinosides. Rat epididymis resembles emulsin except that, as already noted, it lacks beta-glucosidase activity. 4. In the limpet, alpha-l-arabinosidase activity is associated with the enzyme that hydrolyses beta-glucosides and beta-d-fucosides, and not with the separate beta-galactosidase. 5. The effects of the different lactones on the barley preparation suggest that alpha-l-arabinosidase activity is associated with the beta-galactosidase rather than with the enzyme that hydrolyses beta-glucosides and beta-d-fucosides. Fractionation and heat-inactivation experiments indicate that there is also a separate alpha-l-arabinosidase in the preparation.
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PMID:Inhibition of glycosidases by aldonolactones of corresponding configuration. The specificity of alpha-L-arabinosidase. 572 53

1. In barley, beta-glucosidase and beta-galactosidase are separate enzymes. The former also displays beta-d-fucosidase activity. 2. In the limpet, Patella vulgata, beta-glucosidase activity is associated with the beta-d-fucosidase, previously shown to be a separate entity from the beta-galactosidase also present. 3. Almond emulsin presents all three activities as a single enzyme. Each is equally inhibited by glucono-, galactono- and d-fucono-lactone. 4. In rat epididymis, there is no significant beta-glucosidase activity, nor is there appreciable inhibition of the beta-galactosidase and beta-d-fucosidase activities of the preparation by gluconolactone.
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PMID:Inhibition of glycosidases by aldonolactones of corresponding configuration. The C-4- and C-6-specificity of beta-glucosidase and beta-galactosidase. 606 63

The activity levels of beta-N-acetylglucosaminidase, beta-N-acetylgalactosaminidase, beta-galactosidase and beta-glucosidase were fluorometrically assessed in spermatozoa, principal cells, basal cells and fibroblasts isolated from the rat epididymis by centrifugal elutriation. Among the various cell types, corpus principal cells had the highest activities for beta-N-acetylglucosaminidase, beta-N-acetylgalactosaminidase and beta-galactosidase. These enzymes characteristically react with membrane structural carbohydrates. Corpus/caput principal cell activity ratios of these glycosidases remained constant when determinations were done at an alternate pH and substrate concentration, suggesting that similar enzyme forms were present in both regions. Based on cell number and cell volume, sperm glycosidase activities generally increased from the caput to the corpus region of the epididymis, while decreasing from corpus to cauda. However, when data were expressed on the basis of cell protein, sperm glycosidase activities increased from caput to cauda. Since the total protein of sperm decreases dramatically from caput to cauda, the increase in glycosidase activity based on total protein suggests that relative to other sperm proteins, glycosidases may be selectively retained or taken up during epididymal transit. High levels of glycosidase activity associated with the corpus epididymidis may contribute to modification of sperm glycoproteins and observed increases in fertility of sperm as they emerge from this region.
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PMID:Glycosidase activities in principal cells, basal cells, fibroblasts and spermatozoa isolated from the rat epididymis. 643 54

Activity of glycosidases in the epididymis was influenced by several factors originating in the testis. Activities of all the three glycosidases studied viz., beta-glucosidase, beta-galactosidase and alpha-mannosidase were found to be significantly lower in the epididymis of orchidectomized animals than in sham operated rats. However, an enhanced activity of epididymal beta-galactosidase and alpha-mannosidase was noticed in prolactin treated orchidectomized rats compared to orchidectomized rats given vehicle alone. On the other hand, activity of these two enzymes in bromocriptine treated orchidectomized rats was even lower than that found in orchidectomized rats given vehicle. Neither prolactin nor bromocriptine treatment had any significant influence on the epididymal beta-glucosidase. The results suggest a selective but definite action of prolactin on epididymal glycosidases.
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PMID:Modulation in activity of some epididymal glycosidases by prolactin. 835 47

The impact of hyperthyroidism on epididymal glycosidases was studied in albino rats. Hyperthyroidism was induced in Wistar rats aged 30 days by daily injection of T4 (25 microg/100 g body weight/day intramuscularly) for 30 or 60 days; control rats were injected with vehicle (alkaline saline, pH 7.8). One set of hyperthyroid rats was reverted to euthyroid status by withdrawing T4 treatment after 30 days of hyperthyroidism. To asses the direct effect of thyroid hormone on epididymal hexosaminidases, caput, corpus and cauda tissues were stimulated with 25, 50 or 100 ng/mL T3 for 24 h, after an initial culture of 24 h. The activity of beta-glucosidase decreased in caput, corpus and cauda epididymis of hyperthyroid rats. beta-Galactosidase activity increased in the caput epididymis irrespective of the duration of hyperthyroidism. While a similar decrease occurred in the corpus and cauda epididymis in the 30 day hyperthyroid group, an opposite trend was observed in 60 day hyperthyroid rats. Caput beta-N-acetylglucosaminidase activities increased at both time points, whereas activity decreased in the corpus and cauda in 30 day, but increased in 60 day hyperthyroid rats. Hyperthyroidism consistently increased caput and corpus beta-N-acetylgalactosaminidase activity irrespective of the duration. Cauda epididymal beta-N-acetylgalactosaminidase activity was decreased in 30 day and increased in 60 day hyperthyroid rats. Hyperthyroidism induced changes in caput beta-galactosidase, beta-N-acetylgalactosaminidases, corpus beta-N-acetylglucosaminidase and cauda beta-N-acetylgalactosaminidase which were irreversible while the remaining actvities were brought back to normal when T4 treatment was withdrawn. In vitro studies showed that T3 stimulates epididymal hexosaminidases (beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase) irrespective of the dose. These data suggest that thyroid hormones have a specific and direct influence on glycosidases in specific regions of the epididymis.
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PMID:Differential effect of hyperthyroidism on rat epididymal glycosidases. 1145 72

Several 2-(aminomethyl)-and 2-(2-aminoethyl)-pyrrolidine-3,4-diol derivatives have been assayed for their inhibitory activities towards glycosidases. Good inhibitors of alpha-mannosidases must have the (2R,3R,4S) configuration and possess 2-(benzylamino)methyl substituents. Stereomers with the (2S,3R,4S) configuration are also competitive inhibitors of alpha-mannosidases, but less potent as they share the configuration of C(1), C(2), C(3) of beta-D-mannosides rather than that of alpha-D-mannosides. Interestingly, (2S,3R,4S)-2-[2-[(4-phenyl)phenylamino]ethyl]pyrrolidine-3,4-diol (12g) inhibits several enzymes, for instance alpha-L-fucosidase from bovine epididymis (K(i)=6.5microM, competitive), alpha-galactosidase from bovine liver (K(i)=5microM, mixed) and alpha-mannosidase from jack bean (K(i)=102microM, mixed). Diamines such as (2R,3S,4R)-2-[2-(phenylamino) or 2-(benzylamino)ethyl]pyrrolidine-3,4-diol (ent-12a, ent-12b) inhibit beta-glucosidase from almonds (K(i)=13-40microM, competitive).
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PMID:Synthesis and glycosidase inhibitory activities of 2-(aminoalkyl)pyrrolidine-3,4-diol derivatives. 1460 51