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:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It has been known that Hyssopus officinalis (hyssop) is a herb that grows in the wild and is a source of natural antioxidants. We previously reported that a-glucosidase inhibitors, (2S, 3S)1-O-beta-D-6'-O-cinnamoylglucopyranosyl-3-(3", 5"-dimethoxy-4"-hydroxyphenyl)-1,2,3-propanetriol and (2S, 3S)1-O-beta-D-glucopranosyl-3-(3", 5"-dimethoxy-4"-hydroxyphenyl)-1,2,3-propanetriol, from the dry leaves of hyssop, were isolated. This study examined the alpha-glucosidase inhibitory effects of hyssop extracts on intestinal carbohydrate absorption in rat everted gut sac and carbohydrate-loaded hyperglycemia in mice. In the everted gut sac experiment, 10 mM sucrose- and 5 mM maltose-treated increases in glucose concentration in the serosal compartment were inhibited in the presence of 0.5 and 1.0 mg/ mL hyssop extracts, although a 10 mM glucose-induced increase in serosal glucose was not inhibited by the extracts. Additionally, hyperglycemia in sucrose- and maltose-loaded mice was significantly suppressed at an early stage, within 30 to 60 min by oral pre-administration of 300 and 100 mg/kg hyssop extracts, respectively. These findings suggest that hyssop extracts inhibited the digestion of complex carbohydrates, but not that of absorbable monosaccharide, and might be a useful supplemental food for hyperglycemia.
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PMID:Inhibitory effects of hyssop (Hyssopus officinalis) extracts on intestinal alpha-glucosidase activity and postprandial hyperglycemia. 1470 10

The expression of alpha-1,4-glucosidase activity was fluorometrically and electrophoretically assessed in the epididymal fluid and seminal plasma of stallions. alpha-Glucosidase specific activity in the epididymis increased significantly from the proximal caput to the cauda. Stallion epididymal glucosidase maintained activity in a wide range of pH, with two distinct peaks (around pH 4.0 and 6.0, respectively). Enzyme activities at different pH, inhibition assays with sodium dodecyl sulfate (SDS) and maltotriose (MTT, selective inhibitors of alpha-glucosidases "acidic" and "neutral" isoforms, described in other tissues) and the electrophoretic analysis in native and native/SDS-PAGE conditions, indicated that stallion epididymal glucosidase was due to two catalytically active forms. These forms, analyzed by non-denaturing electrophoresis, exhibited different electrophoretic mobility and molecular weight. Samples from the proximal caput of the epididymis were rich in Form II or "neutral" form, whereas the "acid" or Form I seemed to be predominate in the cauda epididymal region. At physiological pH, Form II was predominant in the seminal plasma. The physiological role(s) of these forms is uncertain, but based on their ability to hydrolyze glucosidic linkage, they probably are involved in degradation/modifications of epididymal fluid and/or spermatozoa glycoconjugates, thereby participating in plasma membrane remodeling associated with sperm maturation.
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PMID:Identification and partial characterization of alpha-1,4-glucosidase activity in equine epididymal fluid. 1503 84

Diabetes mellitus is one of the most prevalant diseases of adults. Agents with alpha-glucosidase inhibitory activity have been useful as oral hypoglycemic drugs for the control of hyperglycemia in patients with type 2; noninsulin-dependent, diabetes mellitus (NIDDM). Investigation of some medicinal herbs: Urtica dioica, Taraxacum officinale, Viscum album, and Myrtus communis with alpha-glucosidase inhibitor activity was conducted to identify a prophylactic effect for diabetes in vitro. All plants showed differing potent alpha-glucosidase inhibitory activity. However, Myrtus communis strongly inhibited the enzyme (IC50 = 38 microg/mL). The inhibitory effect of these plants and some common antidiabetic drugs against the enzyme source (baker's yeast, rabbit liver, and small intestine) were also searched. Approximately all inhibitors used in this study showed quite different inhibitory activities, according to alpha-glucosidase origins. Furthermore, subsequent separation of the active material from Myrtus communis by HPLC showed that only one fraction acted as an a-glucosidase inhibitor.
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PMID:Inhibition of alpha-glucosidase by aqueous extracts of some potent antidiabetic medicinal herbs. 1570 95

Long-term type 2 diabetes can lead to numerous biological complications, such as hypertension and cardio-vascular disease. Key enzymes involved in the enzymatic breakdown of complex carbohydrates,pancreatic alpha-amylase and intestinal alpha-glucosidase, have been targeted as potential avenues for modulation of type 2 diabetes-associated post-prandial hyperglycemia through mild inhibition of their enzymatic activities so as to decrease meal-derived glucose absorption. Further, inhibition of hypertension-linked angiotensin I-converting enzyme (ACE) was targeted as a potential approach for modulation of diabetes-linked hypertension. Water-soluble extracts of soybean optimized for phenolic content via sprouting or bioprocessing by dietary fungus (Rhizopus oligosporus, Lentinus edodes) were investigated for inhibitory activity against porcine pancreatic alpha-amylase (PPA), yeast alpha-glucosidase, and rabbit lung ACE in vitro. PPA was allowed to react with each phenolic-optimized extract and the derivatized enzyme-phytochemical mixtures obtained were characterized for residual amylase activity. Alpha-glucosidase and ACE activities were determined in the presence of each phenolic-optimized extract. All of the soybean extracts possessed marked anti-amylase activity, with extracts of R. oligosporus-bioprocessed soybean having the strongest inhibitory activity, but only slight anti-glucosidase activity. The anti-amylase activity of each extract seemed associated with extract antioxidant activity. Anti-enzyme activity was slightly associated with total soluble phenolic content per se, but seemed more associated to the length of sprouting or bioprocessing of the soybean substrate. Short-term sprouting or bioprocessing seemed to improve anti-amylase activity, while long-term sprouting or bioprocessing seemed to aid anti-glucosidase activity. While ACE activity was strongly inhibited by all of the soybean extracts (44-97%), only sprouting was found to increase this inhibition and bioprocessing of soybean with L. edodes decreased inhibitory activity of soybean extract. The results suggest that sprouting and dietary fungal bioprocessing of soybean improve the anti-diabetic potential of soybean extracts, potentially through modulation of the phenolic profile of the extract, and further suggest that enzyme inhibitory activity may be linked to phenolic antioxidant mobilization during spouting and/ or bioprocessing. The significance of food-grade, plant-based enzyme inhibitors for modulation of carbohydrate breakdown and control of glycemic index of foods in the context of preventing hyperglycemia and diabetes mellitus complications such as hypertension in the long-term is hypothesized and discussed.
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PMID:Anti-diabetic and anti-hypertensive potential of sprouted and solid-state bioprocessed soybean. 1592 31

Pompe's disease is a neuromuscular disorder caused by deficiency of lysosomal acid alpha-glucosidase. Recombinant human alpha- glucosidase is under evaluation as therapeutic drug. In light of this development we studied the natural course of cases not fitting the definition of classic infantile Pompe's disease. Our review of 109 reports including 225 cases shows a continuous spectrum of phenotypes. The onset of symptoms ranged from 0 to 71 years. Based on the available literature, no criteria to delineate clinical sub-types could be established.A common denominator of these cases is that first symptoms were related to or caused by muscle weakness. In general, patients with a later onset of symptoms seemed to have a better prognosis. Respiratory failure was the most frequent cause of death. CK, LDH, ASAT, ALAT and muscle glycogen levels were frequently but not always elevated. In most cases a muscle biopsy revealed lysosomal pathology, but normal muscle morphology does not exclude Pompe's disease. In 10% of the cases in which the enzyme assay on leukocytes was used, a normal alpha-glucosidase activity was reported. Data on skeletal muscle strength and function, pulmonary function, disability, handicap and quality of life were insufficiently reported in the literature. Studies of non-classic Pompe's disease should focus on these aspects, before enzyme replacement therapy becomes generally available.
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PMID:The natural course of non-classic Pompe's disease; a review of 225 published cases. 2161 30

The synthesis of analogues of the naturally occurring glycosidase inhibitor, salacinol, in which the D-arabinitol ring has been replaced by D-lyxitol or D-ribitol, is described. Salacinol is one of the active principles in the aqueous extracts of Salacia reticulata, which are traditionally used in India and Sri Lanka for the treatment of Type II diabetes. The synthetic strategy relies on the nucleophilic attack of 1,4-anhydro-2,3,5-tri-O-p-methoxybenzyl-4-thio-D-lyxitol or 1,4-anhydro-2,3,5-tri-O-p-methoxybenzyl-4-thio-D-ribitol at the least hindered carbon of the benzylidene-protected L-cyclic sulfate derived from L-erythritol. Screening of these compounds against recombinant human maltase glucoamylase (MGA), a critical intestinal glucosidase involved in the processing of oligosaccharides of glucose into glucose itself, shows that they are not effective inhibitors of MGA and demonstrates the importance of the d-arabinitol configuration in the heterocyclic ring for effective inhibition.
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PMID:Synthesis of D-lyxitol and D-ribitol analogues of the naturally occurring glycosidase inhibitor salacinol. 1619 22

Lactobacillus brevis is found together with the yeast Brettanomyces lambicus during the overattenuation process in spontaneously fermented lambic beer. An isolated L. brevis strain has been shown to produce an alpha-glucosidase with many similarities to the glucosidase earlier found in B. lambicus. The enzyme was purified by ammonium sulfate precipitation, gel (Sephadex G-150 and Ultrogel AcA-44) filtration, and ion-exchange chromatography (DEAE-Sephadex A-50). The molecular weights of the enzyme, as determined by gel chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were about 50,000 and 60,000, respectively. Optimum catalytic activity was obtained at 40 degrees C and pH 6.0. The enzyme showed a decrease of hydrolysis with an increase in the degree of polymerization of the substrate. The K(m) values for p-nitrophenyl-alpha-d-glucopyranoside, maltose, and maltotriose were 0.51, 3.0, and 5.2 mM, respectively. There was lack of inhibition by 0.15 mM acarbose and 0.5 M turanose, but the enzyme was inhibited by Tris (K(i) value of 25 mM). The alpha-glucosidase of L. brevis together with the enzyme of B. lambicus seems to be a key factor in the overattenuation of lambic beer, although the involvement of other lactic acid bacteria (pediococci) cannot be excluded.
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PMID:Localization and Characterization of alpha-Glucosidase Activity in Lactobacillus brevis. 1634 68

Four chain extended homologues of salacinol, a naturally occurring glycosidase inhibitor, were prepared for evaluation as inhibitors of glucosidase enzymes involved in the breakdown of carbohydrates. The syntheses involved the reactions of 1,4-anhydro-2,3,5-tri-O-benzyl-4-thio-D-arabinitol with cyclic sulfate derivatives of different monosaccharides. Debenzylation of the products afforded the novel sulfonium sulfate derivatives of D-glucose, D-galactose, D-arabinose, and D-xylose that are of interest in their own right as glycosidase inhibitors. Reduction to the corresponding alditols then afforded the homologues of salacinol containing polyhydroxylated, acyclic chains of 5- and 6-carbons, differing in stereochemistry at the stereogenic centers. Three of the chain-extended homologues inhibited recombinant human maltase glucoamylase, one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine, with Ki values in the low micromolar range, of approximately the same magnitude as salacinol, thus providing lead candidates for the treatment of Type 2 diabetes.
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PMID:Synthesis of sulfonium sulfate analogues of disaccharides and their conversion to chain-extended homologues of salacinol: new glycosidase inhibitors. 1643 29

The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (alpha-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II alpha-glucosidase. The optimum temperature of the enzyme was 70 degrees . In addition, the enzyme was highly thermostable (100% stability for 10 h at 60 degrees and a half-life of 15 min at 80 degrees), and stable within a wide pH range.
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PMID:A specific short dextrin-hydrolyzing extracellular glucosidase from the thermophilic fungus Thermoascus aurantiacus 179-5. 1682 Jul 57

The syntheses of nine S-alkylated, cyclic sulfonium-ions with varying alkyl chain lengths, as mimics of N-alkylated imino sugars, and their glucosidase inhibitory activities are described. The target compounds were synthesized by alkylation of 2,3,5-tri-O-benzyl-1,4-anhydro-4-thio-d-arabinitol at the ring sulfur atom using various alkyl halides, followed by deprotection using boron trichloride. Enzyme inhibitory assays against recombinant human maltase glucoamylase (MGA), a critical enzyme in the small intestine involved in the breakdown of glucose oligosaccharides into glucose itself, shows that they are effective inhibitors of MGA with K(i) values ranging from 6 to 75 microM.
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PMID:Synthesis of S-alkylated sulfonium-ions and their glucosidase inhibitory activities against recombinant human maltase glucoamylase. 1731 80


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