Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mechanism by which the fertilization envelope (FE) is able to protect the embryo of fish until hatching is almost unknown, except for its function as a physical barrier. FE extract from activated or fertilized eggs of the fish Salmo gairdneri was demonstrated to contain enzyme activities using an agar plate enzyme assay. The enzymes apparently active were carboxymethylcellulase (cellulase; EC 3.2.1.4), laminaranase (endo-1,3(4)-beta-glucanase; EC 3.2.1.6), carboxymethylchitinase (chitinase; EC 3.2.1.14), xylanase (endo-1,4-beta-xylanase; EC 3.2.1.8), mannanase (mannan 1,2-(1,3)-alpha-mannosidase; EC 3.2.1.77), dextranase (EC 3.2.1.11), a protease and lysozyme (EC 3.2.1.17). The FE extract exerted an antifungal or fungicidal action on the fungus Saprolegnia parasitica, whereas an extract from the vitelline envelopes (VE) has no apparent enzyme activity nor antifungal or fungicidal action. Enzymes acquired by the FE through the cortical reaction may have an important defensive role, protecting the embryo against invaders or pathogens.
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PMID:Enzymatic basis for protection of fish embryos by the fertilization envelope. 154 61

The nucleotide sequence of an 852 base pair (bp) DNA fragment containing the entire gene coding for thermostable beta-1,3-1,4-glucanase of Bacillus macerans has been determined. The bglM gene comprises an open reading frame (ORF) of 711 bp (237 codons) starting with ATG at position 93 and extending to the translational stop codon TAA at position 804. The deduced amino acid sequence of the mature protein shows 70% homology to published sequences of mesophilic beta-1,3-1,4-glucanases from B. subtilis and B. amyloliquefaciens. The sequence coding for mature beta-glucanase is preceded by a putative signal peptide of 25 amino acid residues, and a sequence resembling a ribosome-binding site (GGAGG) before the initiation codon. By contrast with the processed protein, the N-terminal amino acid sequence constituting the putative leader peptide bears no or only weak homology to signal peptides of mesophilic Bacillus endo-beta-glucanases. The B. macerans signal peptide appears to be functional in exporting the enzyme to the periplasm in E. coli. More than 50% of the whole glucanase activity was localized in the periplasmic space and in the supernatant. Whereas homology to endo-1,4-beta-glucanases is completely lacking, a weak amino acid homology between the sequence surrounding the active site of phage T4 lysozyme and a sequence spanning residues 126 through 161 of B. macerans endo-beta-glucanase could be identified.
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PMID:Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases. 227 30

Optimal conditions for the formation and isolation of protoplasts from the fungus Penicillium brevi-compactum were investigated. Localization of ribonuclease, glucosoisomerase and beta-1,3-glucanase in the mycelium was examined. To produce protoplasts, the mycelium was treated for 3-4 hours at 40 degrees C with the incubation mixture, containing chitinase from Actinomyces kurssanovii, lytic enzymes from Act. cellulose, lysozyme and 0.8 M mannitol as an osmotic stabilizer. The levels of activities of RNase, beta-1,3-glucanase, and glucosoisomerase were measured in the fungal mycelium before preparation of protoplasts, in the incubation mixture after their preparation, and in the protoplast lysate. The protoplast formation facilitated the release of RNase, beta-1,3-glucanase and glucosoisomerase from the fungal mycelium into the incubation mixture.
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PMID:[Preparation of protoplasts and localization of ribonuclease, beta-1,3-glucanase and glucosoisomerase in the fungal mycelium of Penicillium brevi-compactum]. 738 13

Chickpea (Cicer arietinum L.) cell-suspension cultures were used to isolate one beta-1,3-glucanase (EC 3.2.1.29) and two chitinases (EC 3.2.1.14). The beta-1,3-glucanase (M(r) = 36 kDa) and one of the chitinases (M(r) = 32 kDa) belong to class I hydrolases with basic isoelectric points (10.5 and 8.5, respectively) and were located intracellularly. The basic chitinase (BC) was also found in the culture medium. The second chitinase (M(r) = 28 kDa), with an acidic isoelectric point of 5.7, showed homology to N-terminal sequences of class III chitinases and represented the main protein accumulating in the culture medium. Polyclonal antibodies raised against the basic beta-1,3-glucanase (BG) and the acidic chitinase (AC) were shown to be monospecific. The anti-AC antiserum failed to recognize the BC on immune blots, confirming the structural diversity between class I and class III chitinases. Neither chitinase exhibited lysozyme activity. All hydrolases were endo in action on appropriate substrates. The BC inhibited the hyphal growth of several test fungi, whereas the AC failed to show any inhibitory activity. Expression of BG activity appeared to be regulated by auxin in the cell culture and in the intact plant. In contrast, the expression of neither chitinase was apparently influenced by auxin, indicating a differential hormonal regulation of beta-1,3-glucanase and chitinase activities in chickpea. After elicitation of cell cultures or infection of chickpea plants with Ascochyta rabiei, both system were found to have hydrolase patterns which were qualitatively and quantitatively comparable.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Purification, characterization and differential hormonal regulation of a beta-1,3-glucanase and two chitinases from chickpea (Cicer arietinum L.). 776 57

An acidic beta-1,3-glucanase was detected in cucumber leaves inoculated with either Colletotrichum lagenarium or tobacco necrosis virus (TNV) as well as in the leaves above those inoculated with the pathogens. The enzyme is extracellular and migrates in native polyacrylamide gel electrophoresis (PAGE) together with a Class III chitinase, a bifunctional chitinase/lysozyme. The beta-1,3-glucanase was separated by ultra-narrow pH range IEF-PAGE or by SDS_PAGE and was purified to apparent homogeneity. Only one isoform of the enzyme was detected. Its apparent molecular mass in 38 kDa as estimated by SDS-PAGE, its isoelectric point is 3.6 and the specific activity is approximately 26 micromol glucose equivalents liberated from laminarin min(-1)mg(-1) protein. Partial amino acid (five peptide fragments with a total of 65 amino acids) sequencing of the beta-1,3-glucanase revealed similarities of 49% to 72% to sequences of published beta-1,3-glucanases from tobacco, tomato, soybean, barley, and rice plants. A time course study indicated that the increase of the beta-1,3-glucanase activity was associated with induced resistance against C. lagenarium. The implications of these results to coordinate defense responses in plant-microbe interactions are discussed.
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PMID:Purification and characterization of an acidic beta-1,3-glucanase from cucumber and its relationship to systemic disease resistance induced by Colletotrichum lagenarium and tobacco necrosis virus. 866

The lutoid-body (bottom) fraction of latex from the rubber tree (Hevea brasiliensis) contains a limited number of major proteins. These are, besides the chitin-binding protein hevein, its precursor and the C-terminal fragment of this precursor, proteins with enzymic activities: three hevamine components, which are basic, vacuolar, chitinases with lysozyme activity, and a beta-1,3-glucanase. Lutoid-body fractions from three rubber-tree clones differed in their contents of these enzyme proteins. The hevamine components and glucanase were isolated and several enzymic and structural properties were investigated. These enzymes are basic proteins and cause coagulation of the negatively charged rubber particles. The coagulation occurs in a rather narrow range of ratios of added protein to rubber particles, which indicates that charg neutralization is the determining factor. Differences in coagulation of rubber particles by lutoid-body fractions from various rubber clones can be explained by their content of hevamine and glucanase. Glucanase from the lutoid-body fraction may dissolve callus tissue and this may explain the observation that rubber-tree clones with a high glucanase content in this fraction produce more latex than clones with little glucanase. Sequence studies of two CNBr peptides of the glucanase indicate that this protein is homologous with glucanases from other plants, and that a C-terminal peptide, possibly involved in vacuolar targeting, may have been cleaved off.
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PMID:Chitinase and beta-1,3-glucanase in the lutoid-body fraction of Hevea latex. 898 4

Immediate-type allergic reactions to latex products made from natural rubber are called latex allergy. One of the notable features of latex-allergic people is their cross-reactivity to various vegetable foods and pollen. The structurally similar proteins which most kinds of plants potentially induce must be responsible for these cross-reactions. However, the taxonomical dissimilarity among the causative plants has kept us from concrete explanations of such cross-reactive allergens. We have speculated that plant defense-related proteins are a possible cause of the latex allergy. The well-known serologic relationships and sequence similarities of these ubiquitous plant proteins can explain the cross-reactivity without difficulty. Rubber trees cultured in plantation farms are repeatedly tapped and treated with phytohormones. These stresses would result in the significant induction of defense-related proteins. Indeed, we were able to detect defense-related enzymes in latex extracts. Moreover, three hydrolytic enzymes (beta-1,3-glucanase, chitinase/lysozyme, and carboxylesterase) that are very likely to take a defensive role were specifically recognized by the IgE antibodies of latex-allergic people and atopic patients. These experimental results strongly support our hypothesis. Because of their conserved structures, defense-related proteins should form a family of plant pan-allergens.
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PMID:[Plant defense-related proteins as latex allergens]. 1009 12

Tenebrio molitor larvae were successfully reared free of cultivatable gut lumen bacteria, yeasts and fungi using two approaches; aseptic rearing from surface sterilized eggs and by feeding larvae with antibiotic-containing food. Insects were reared on a rich-nutrient complete diet or a nutrient-poor refractory diet. A comparison of digestive enzyme activities in germ free and conventional insects containing a gut microbiota did not reveal gross differences in enzymes that degrade cell walls from bacteria (lysozyme), fungi (chitinase and laminarinase) and plants (cellulase and licheninase). This suggested that microbial-derived enzymes are not an essential component of the digestive process in this insect. However, more detailed analysis of T. molitor midgut proteins using an electrophoretic separation approach showed that some digestive enzymes were absent and others were newly expressed in microbiota-free larvae. Larvae reared in antibiotic-containing refractory wheat bran diet performed poorly in comparison with controls. The addition of saligenin, the aglycone of the plant glucoside salicin, has more deleterious effects on microbiota-free larvae than on the conventionally reared larvae, suggesting a detoxifying role of midgut microbiota. Analysis of the volatile organic compounds released from the faecal pellets of the larvae shows key differences in the profiles from conventionally reared and aseptically reared larvae. Pentadecene is a semiochemical commonly found in other beetle species. Here we demonstrate the absence of pentadecene from aseptically reared larvae in contrast to its presence in conventionally reared larvae. The results are discussed in the light of the hypothesis that microbial products play subtle roles in the life of the insect, they are involved in the digestion of refractory food, detoxification of secondary plant compounds and modify the volatile profiles of the insect host.
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PMID:Potential role for gut microbiota in cell wall digestion and glucoside detoxification in Tenebrio molitor larvae. 1660 Feb 86

Chitinase and beta-1,-3-glucanase activities increased coordinately in pea (Pisum sativum L. cv "Dot") pods during development and maturation and when immature pea pods were inoculated with compatible or incompatible strains of Fusarium solani or wounded or treated with chitosan or ethylene. Up to five major soluble, basic proteins accumulated in stressed immature pods and in maturing untreated pods. After separation of these proteins by chromatofocusing, an enzymic function could be assigned to four of them: two were chitinases and two were beta-1,3-glucanases. The different molecular forms of chitinase and beta-1,3-glucanase were differentially regulated. Chitinase Ch1 (mol wt 33,100) and beta-1,3-glucanase G2 (mol wt 34,300) were strongly induced in immature tissue in response to the various stresses, while chitinase Ch2 (mol wt 36,200) and beta-1,3-glucanase G1 (mol wt 33,500) accumulated during the course of maturation. With a simple, three-step procedure, both chitinases and both beta-1,3-glucanases were purified to homogeneity from the same extract. The two chitinases were endochitinases. They differed in their pH optimum, in specific activity, in the pattern of products formed from [(3)H]chitin, as well as in their relative lysozyme activity. Similarly, the two beta-1,3-glucanases were endoglucanases that showed differences in their pH optimum, specific activity, and pattern of products released from laminarin.
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PMID:Antifungal Hydrolases in Pea Tissue : I. Purification and Characterization of Two Chitinases and Two beta-1,3-Glucanases Differentially Regulated during Development and in Response to Fungal Infection. 1666 42

Inoculation of mature leaves of turnip (Brassica campestris) with the incompatible Xanthomonas campestris pv vitians resulted in the induction of beta-1,3-glucanase and chitinase/lysozyme (CHL) activity. No increase in the basal activity of beta-1,3-glucanase was observed after inoculation of leaves with heat- or rifampicin-killed X. c. vitians, Escherichia coli, or sterile water. Inoculation with the compatible X. campestris pv campestris resulted in a slower induction of glucanase than that seen with X. c. vitians. In contrast, all bacteria caused an induction of CHL activity. One major beta-1,3-glucanase (molecular mass 36.5 kilodaltons, isoelectric point [pl] ~8.5) was purified from both inoculated and untreated leaves by ion-exchange chromatography. The enzyme degraded laminarin by an endo-glycolytic mechanism. Two major CHL isozymes (CHL 1 and CHL 2, molecular mass 30 kilodaltons and pl 9.4 and 10.2, respectively) were purified from X. c. vitians inoculated leaves by affinity chromatography on a chitin column followed by ion-exchange chromatography. Both enzymes degraded chitin by an endo-glycolytic mechanism although the ratio of lysozyme to chitinase specific activities for CHL 1 and CHL2 were different. The induction of CHL 1 was associated with the hypersensitive reaction caused by X. c. vitians whereas all other treatments induced largely CHL 2.
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PMID:Induction of Hydrolytic Enzymes in Brassica campestris in Response to Pathovars of Xanthomonas campestris. 1666 41


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