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:3.2.1.21 (beta-glucosidase)
3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A variety of lectins were tested in vitro for inhibitory action against the activities of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase and the N-glycohydrolases (alpha-glucosidase, beta-glucosidase and beta-glucuronidase). Lectins from Phaseolus vulgaris, Momordica charantia, Ricinus communis and its constituent chains, and Agaricus bisporus were able to inhibit HIV-1 reverse transcriptase. P. vulgaris lectin and A. bisporus lectin were the most potent. The aforementioned lectins had only weak or no inhibitory effects on the glycohydrolases. The inhibitory effect of polysaccharopeptide from the mushroom Coriolus versicolor on HIV-1 reverse transcriptase and alpha-glucosidase was enhanced after chemical modification with chlorosulfonic acid. However, the inhibitory effect of the algal polysaccharide fucoidan on HIV-1 reverse transcriptase and alpha-glucosidase was not augmented by sulfation. Trypsin inhibitors from Phaseolus lunatus and Glycine max, gossypol and alkaloids from Corydalis yanhusuo were able to inhibit HIV-1 reverse transcriptase. Dicoumarol was capable of inhibiting HIV-1 reverse transcriptase, alpha-glucosidase, beta-glucosidase and beta-glucuronidase.
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PMID:Examination of lectins, polysaccharopeptide, polysaccharide, alkaloid, coumarin and trypsin inhibitors for inhibitory activity against human immunodeficiency virus reverse transcriptase and glycohydrolases. 1158 48

The activities of alpha-glucosidase, beta-glucosidase, and beta-galactosidase were studied during the isolation and purification of lectins from Azospirillum brasilense Sp7 and Azospirillum lipoferum 59b cells. These enzymatic activities were revealed in crude extracts of surface proteins, protein fraction precipitated with ammonium sulfate or ethanol-acetone mixture, and protein fraction obtained by gel filtration on Sephadex G-75. The distribution of the enzymes between different protein fractions varied among the azospirilla studied. The cofunction of the A. brasilense Sp7 lectin and beta-galactosidase on the cell surface is assumed. A strong interaction between the A. lipoferum 59b lectin and glucosidases was revealed. The lectin from A. lipoferum 59b may possess saccharolytic activity.
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PMID:[Relationship between lectin, alpha-, beta-glucosidase, and beta-galactosidase activities of Azospirillum]. 1176 84

Enzyme-lectins LI and LII from Paenibacillus polymyxa 1460, when incubated with the carbohydrate moiety of the wheat-root exocomponent fraction, showed an increase in their proteolytic activity. This increase may be associated with the presence of lectin-specific carbohydrates in the root fraction. The lectins of the nitrogen-fixing paenibacilli enhance cellulose degradation in the plant cell, thus increasing the activity of beta-glucosidase in the wheat-root cell wall.
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PMID:Biological role of lectins from the nitrogen-fixing Paenibacillus polymyxa strain 1460 during bacterial-plant-root interactions. 1466 12

Plant cells develop various types of endoplasmic reticulum (ER)-derived structures with specific functions. ER body, an ER-derived compartment in Arabidopsis thaliana, is a spindle-shaped structure. The NAI1 gene regulates the development of ER bodies because mutation of NAI1 abolishes the formation of ER bodies. To better understand the role of NAI1, we cloned the NAI1 gene using a positional cloning strategy. The nai1-1 mutant had a single nucleotide change at an intron acceptor site of At2g22770 (NAI1 gene). Because of this mutation, aberrant splicing of NAI1 mRNA occurs in the nai1-1 mutant. NAI1 encodes a transcription factor that has a basic-helix-loop-helix (bHLH) domain. Transient expression of NAI1 induced ER bodies in the nai1-1 mutant. Two-dimensional electrophoresis and RT-PCR analyses showed that a putative lectin was depressed at both the mRNA and protein levels in nai1 mutants, as was a beta-glucosidase (PYK10). Our results provide direct evidence that a bHLH protein plays a role in the formation of ER bodies.
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PMID:NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body. 1515 89

Corn coleoptile lectin is present with beta-glucosidase (EC. 3.2.1.2.1) in a single tightly bound molecular association complex (88.7 kDa). SDS-PAGE of the molecular complex dissociates into two main components. Of these, at a concentration of 75%, the corn coleoptile beta-glucosidase (60 kDa) is identified by enzymatic activity, with two 16-amino acid tryptic peptides displaying close homology with the primary structure of the enzyme. In separate experiments, we isolated homogenous monomeric enzyme of corn coleoptile. This allowed us to conclude that lectin properties like erythrocyte agglutination, found in the (88.7 kDa) molecular complex, is not due to the beta-glucosidase bound in it. Another protein (30 kDa) dissociated from the same SDS-PAGE gels rendered several tryptic peptides, including a 20-amino acid sequence V(L)GP(Q)W(A)GGSGGSPVDITAEPQR closely homologous to the putative beta-glucosidase aggregating factor (BGAF) precursor described recently. Tryptic peptide SAFTE(A)WN(V)ELK(V) was also present in the BGAF precursor. KFHEQR peptide was not present in BGAF precursor or any other protein sequence examined. Tryptic peptide TYGPFGA showed good homology with the BGAF precursor protein, FEGLYLFHTPLGSGAN peptide displayed identity with the BGAF precursor sequence. Thus, the 30 kDa protein does not appear to be identical to BGAF, but is rather a similar molecule which could be endowed with the lectin properties of the 88.7 kDa molecular complex.
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PMID:Molecular association of lectin and beta-glucosidase in corn coleoptile. 1554 Dec 99

Jasmonates are distributed throughout higher plants, where they play an important role in the activation of signal transduction pathways in response to wounding and pathogen attack. Jasmonates are known to induce the transcriptional activation of plant defense genes, produce jasmonate-regulated proteins (JRP). One class of 32 kDa JRP (designated as JRP-32 in this paper) is present in the Gramineae family, although the function of these proteins is still unclear. A cDNA was cloned from wheat (Triticum aestivum L.) and designated as Ta-JA1. Sequence comparison indicated that Ta-JA1 encodes a JRP-32 protein. Ta-JA1 exists as a single-copy gene, but other genes with low sequence similarity to Ta-JA1 may be present in the wheat genome. The expression of Ta-JA1 was confined to stem tissues and barely detected in leaf and root tissues. Western blot analyses demonstrated that the recombinant Ta-JA1 protein cross-reacts with maize beta-glucosidase-aggregating factor (BGAF) antibody. Molecular modeling showed that Ta-JA1 and BGAF have a very similar three-dimensional structure. Protein structure analysis indicated that Ta-JA1 together with some related proteins (maize BGAF, wheat Ver2, WCI-1 and Hfr-1) contain two functional domains: a disease response domain and jacalin-related lectin (JRL) domain. A mannose-binding site was also well conserved in these proteins. The data support the hypothesis that JRP-32 and related proteins from Gramineae form a small protein family related to JRLs. This small protein family may have evolved from mannose-specific jacalin-related lectins (mJRLs) by developing a disease response domain in their N-terminus, which may have broadened the functional role of these proteins to include the plant defense response.
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PMID:Characterization of a jasmonate-regulated wheat protein related to a beta-glucosidase-aggregating factor. 1582 Jun 67

The infective third-stage larvae (L3s) of Strongyloides ratti, a parasitic nematode in rodents, showed two types of chemokinesis on a gradient of sodium chloride (NaCl) in an in vitro agarose tracking assay. The types were a consistent directional avoidance behavior under unfavorable environmental conditions and a reduced avoidance behavior under favorable conditions. We examined the effects of treatments with glycolytic enzymes and lectins by analyzing the avoidance behavior. L-Fucose dehydrogenase, hyaluronidase, beta-glucosidase, alpha-mannosidase, beta-galactosidase, concanavalin A, wheat germ agglutinin and soybean agglutinin exhibited inhibitory or enhancive effects on chemokinesis. We also confirmed the sites of the amphids of L3s aside from the mouth at the anterior end by scanning electron microscopy, and that concanavalin A-binding sites existed in the vicinity of the amphids using lectin-histochemistry. The carbohydrate moieties in the amphids of S. ratti L3s may play an important role as chemosensors in perceiving environmental cues.
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PMID:Strongyloides ratti: chemokinesis of glycolytic enzyme- and lectin-treated third-stage infective larvae in vitro. 1586 77

The ER body is an endoplasmic reticulum (ER)-derived organelle. Because ER bodies are induced by wounding and methyl jasmonate (MeJA) treatment in rosette leaves, they might be responsible for defense systems. Recently, we isolated nai1 mutants that have no ER body and showed that the levels of PYK10 and PBP1 (PYK10-binding protein 1: At3g16420) were decreased in nai1 mutants. PYK10 is a beta-glucosidase that is localized in ER bodies. PBP1 consists of two repeated regions, each of which is highly homologous to the alpha-chain of jacalin, a carbohydrate-binding protein (lectin) of Artocarpus integriforia. We show in this study that PYK10 has two forms, an active form and an inactive form. The amount of active form increased during incubation of root homogenate. On the other hand, PYK10 separated into soluble and insoluble forms. Active PYK10 molecules mainly occurred as the insoluble form and inactive PYK10 molecules remain soluble. This suggests that the activation of PYK10 needs polymerization. In homogenates of both a pbp1 mutant and the wild type, PYK10 becomes insoluble, while PYK10 activity in pbp1 is only half of that in the wild type. PBP1 has an ability to interact with PYK10. Nonetheless, PBP1 does not bind active PYK10. These results suggest that PBP1 has some effect on the activation of PYK10. In addition, PBP1 was found to have a different subcellular distribution from PYK10. PBP1 may act like a molecular chaperone that facilitates the correct polymerization of PYK10, when tissues are damaged and subcellular structures are destroyed by pests.
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PMID:Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana. 1591 74

Lineage-specific gene loss is considered one of the processes contributing to speciation and genome diversity. Such gene loss has been inferred from interspecies comparisons of orthologous DNA segments. Examples of intraspecific gene loss are rare. Here we report identification of a gene, designated Crs-1 (creeping specific-1), that appears to be in the process of being lost from heterozygous populations of the species creeping bentgrass (Agrostis stolonifera). The Crs-1 gene encodes a protein with an N-terminal dirigent protein domain and a C-terminal lectin domain and is similar to the maize (Zea mays) beta-glucosidase aggregating factor. Most individual creeping bentgrass plants examined are lacking Crs-1. Some individuals are hemizygous for the Crs-1 locus, indicating major haplotype noncolinearity at that locus. Crs-1 was not detected in several other Agrostis species, indicating it is being lost from the genus. The Crs-1 locus in creeping bentgrass provides a rare example of the evolutionary process of gene loss occurring within a plant species.
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PMID:Identification of a gene in the process of being lost from the genus Agrostis. 1599 2

To understand the mechanisms of aluminum (Al) tolerance in wheat (Triticum aestivum L.), suppression subtractive hybridization (SSH) libraries were constructed from Al-stressed roots of two near-isogenic lines (NILs). A total of 1,065 putative genes from the SSH libraries was printed in a cDNA array. Relative expression levels of those genes were compared between two NILs at seven time points of Al stress from 15 min to 7 days. Fifty-seven genes were differentially expressed for at least one time point of Al treatment. Among them, 28 genes including genes for aluminum-activated malate transporter-1, ent-kaurenoic acid oxidase-1, beta-glucosidase, lectin, histidine kinase, and phospoenolpyruvate carboxylase showed more abundant transcripts in Chisholm-T and therefore may facilitate Al tolerance. In addition, a set of genes related to senescence and starvation of nitrogen, iron, and sulfur, such as copper chaperone homolog, nitrogen regulatory gene-2, yellow stripe-1, and methylthioribose kinase, was highly expressed in Chisholm-S under Al stress. The results suggest that Al tolerance may be co-regulated by multiple genes with diverse functions, and those genes abundantly expressed in Chisholm-T may play important roles in enhancing Al tolerance. The down-regulated genes in Chisholm-S may repress root growth and restrict uptake of essential nutrient elements, and lead to root senescence.
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PMID:Transcriptional analysis between two wheat near-isogenic lines contrasting in aluminum tolerance under aluminum stress. 1703 77


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