Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mycelial and yeast forms of P. brasiliensis were tested for several glucohydrolases. In addition to high levels of beta-glucanases, low amounts of alpha-glucanase, chitinase and maltase were found. Tests for invertase, amylase and lactase were negative. The levels of beta-1,3-glucanase were higher in the mycelial form. The shift to the mycelial phase correlated with an increase in the levels of beta-1,3-glucanase. The enzyme was present in the cytoplasm, cell wall and culture medium. The extracellular enzyme was purified 42 fold by ammonium sulphate precipitation and gel filtration. Maximal activity was obtained at 60 degrees C and pH of 5.0 (acetate buffer or pH 6.0 (phosphate buffer). Its Km was 0.205 mg/ml. The cell wall-bound enzyme showed a higher temperature optimum. Optimum pH and Km were also slightly different. Following treatment of the cell walls with chitinase, beta-1,3-glucanase was released into the medium.
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PMID:Beta-1-3-glucanase and dimorphism in Paracoccidioides brasiliensis. 4 May 30

beta-Glucanases secreted into culture fluid by protoplasts or intact cells of the yeast Saccharomyces cerevisiae were investigated for the presence of covalently linked carbohydrates. Gel filtration of the enzymes on Biogel A-1.5m showed that endo-beta-1,3-glucanase is a polydisperse enzyme of high-molecular weight which elutes in about the same volume as external yeast invertase. Exo-beta-glucanase was eluted from the gel as a much lighter enzyme. Endo-beta-1,3-glucanase added to a mixture of extracellular mannoproteins was precipitated by concanavalin A to a similar extent to mannan, invertase and acid phosphatase. Under the same conditions exo-beta-glucanase did not interact with the lectin, but was partially precipitated from the solution in the absence of foreign mannan or mannan-proteins. The results show that endo-beta-1,3-glucanase of S. cerevisiae is a mannoprotein of a similar nature to external invertase and acid phosphatase. However, exo-beta-glucanase appears to be a glycoprotein which does not contain the highly branched mannan polymer in its molecule.
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PMID:Interaction of concanavalin A with external mannan-proteins of Saccharomyces cerevisiae. Glycoprotein nature of beta-glucanases. 79 52

Brock, Thomas D. (Indiana University, Bloomington). Biochemical and cellular changes occurring during conjugation in Hansenula wingei. J. Bacteriol. 90:1019-1025. 1954.-A technique has been devised for deagglutinating mixed populations of conjugating cells so as to be able to visualize microscopically early stages of the conjugation process. A cell can form a conjugation tube only when in contact with a cell of opposite mating type, but may do so even if the mate is unresponsive or ultraviolet-inactivated. Cell fusion occurs, however, only when both cells are able to form conjugation tubes in a region of contact. Fusion begins almost as soon as the two cells begin to form protuberances, and long before any dissolution of cell-wall material between the cells occurs. A cell which has conjugated in one region of its cell wall is still able to conjugate with another cell in another region, so that triply and quadruply conjugated cells are occasionally formed. There is no significant net increase in deoxyribonucleic acid, ribonucleic acid, protein, or carbohydrate which might be related to the conjugation process, because any minor changes that occur in these components are also detected when cells of only one mating type are incubated or when the conjugation process is inhibited with the antibiotic cycloheximide. Changes in activity of beta-1,3-glucanase (with laminarin as substrate) and beta-1,6-glucanase (with pustulan as substrate) have been measured during the conjugation process, in addition to changes in the activity of several control enzymes which would not be expected to be related to the conjugation process. Significant increases in invertase (sucrase), laminarinase, and pustulanase were detected, and minimal increases occurred in beta-glucosidase and acid phosphatase. However, these same increases were also observed in controls involving only one mating type; thus, these increases are probably not related to the conjugation process, but may be a result of other processes which probably occur during incubation in the conjugation medium.
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PMID:Biochemical and cellular changes occuring during conjugation in Hansenula wingei. 584 91

A DNA segment encoding a signal peptide from yeast invertase was fused in frame to bglH gene encoding 87-kD-beta-1,3-glucanase from Bacillus circulans IAM1165 and was expressed in the yeast Saccharomyces cerevisiae under the control of the GAL1 gene promoter. Yeast cells containing this fused gene produced active beta-1,3-glucanase in the medium after a long period of incubation at low temperature. The enzyme produced by yeast was heterogeneous in size, and larger than the enzyme produced by Escherichia coli.
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PMID:Expression of an 87-kD-beta-1,3-glucanase of Bacillus circulans IAM1165 in Saccharomyces cerevisiae by low-temperature incubation. 776 62

The sexual adhesion protein of Saccharomyces cerevisiae MAT alpha cells, alpha-agglutinin, could not be extracted from the cell wall with hot sodium dodecyl sulfate (SDS), but became soluble after digestion of the cell wall with laminarinase. This indicates that it is intimately associated with cell wall glucan. A fusion protein was constructed consisting of the signal sequence of yeast invertase, guar alpha-galactosidase, and the C-terminal half of the alpha-agglutinin. Most of the fusion protein was incorporated in the cell wall. A small amount could be extracted with SDS, but most of it could only be extracted with laminarinase. On the other hand, cells containing a construct consisting of the signal sequence of invertase and alpha-galactosidase released most of the alpha-galactosidase into the medium and all cell wall-associated alpha-galactosidase was released by SDS. Labelling with antibodies showed that the alpha-galactosidase part of the fusion protein was exposed on the surface of the cell wall. The results demonstrate that the C-terminal half of the alpha-agglutinin contains the information needed to incorporate a protein into the cell wall.
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PMID:Targeting of a heterologous protein to the cell wall of Saccharomyces cerevisiae. 839 Jan 28

Taking two cotton cultivars with different fiber strength (KC-1, average fiber strength 35 cN x tex(-1); and AC-33B, average fiber strength 32 cN x tex(-1)) as test materials, a field experiment with two planting dates (25 April and 25 May) was conducted in Nanjing of Jiangsu (lower reaches of Yangtze River Valley) and Xuzhou of Jiangsu (Yellow River Valley) to study the dynamic changes of plant sucrase, sucrose synthase, sucrose phosphate synthase, and beta-1,3-glucanase activities during the development of cotton fiber at different air temperatures and their relationships with fiber length and strength. In the development period of fiber elongation, sucrase and beta-1,3-glucanase activities were higher; while during the period of fiber thickening, sucrose synthase and sucrose phosphate synthase activities increased rapidly and were high, but sucrase and beta-1,3-glucanase activities had a rapid decrease. The higher sucrase activity in fiber elongation development period favored the fiber length development, while the rapid increase of sucrose synthase and sucrose phosphate synthase and the rapid decrease of sucrase and beta-1,3-glucanase activity favored the development of fiber strength. For cotton variety KC-1, the sucrase and beta-1,3-glucanase activities in its early development period and the sucrose synthase and sucrose phosphate synthase activities in its middle and later development periods were all higher than those of AC-33B. In this study, 23.3 degrees C was the optimal temperature for high strength fiber formation, and 23.3 degrees C - 25.5 degrees C was the optimal temperature for long length fiber formation.
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PMID:[Effects of air temperature on enzyme activities of cotton plants related to saccharide metabolism of cotton fiber]. 1944 79

Taking two cotton cultivars with difterent temperature-sensitivity during tneir liner strength formation as test materials, a field experiment of different sowing dates was conducted in Nanjing of Jiangsu Province in 2006 and 2007 to study the effects of low temperature on the activities and gene expression of the enzymes related to fiber development. The low temperature induced by late sowing (with the mean daily minimum temperature being 21.1, 20.5, and 18.1 degrees C during fiber development period) had definite effects on the enzyme activities, and accordingly, the fiber strength formation. Low temperature increased the invertase and beta-1, 3-glucanase activities, decreased the sucrose synthase and sucrose phosphate synthase activities, prolonged the time with higher gene expression level of Expansin and sucrose synthase, and delayed the expression peak and decreased the gene expression quantity of beta-1,3-glucanase. There existed significant differences in the low-temperature responses of related enzymes activities between the two cultivars, with the change ranges of the enzyme activities being larger for temperature-sensitive cultivar Sumian 15 than for temperature-insensitive cultivar Kemian 1, which could be the main reasons leading to the different temnerature-sensitivitv of the two cotton cultivars during their fiber strength formation.
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PMID:[Low-temperature responses of enzyme activities related to fiber development of two cotton (Gossvpium hirsutum L.) cultivars with different temperature-sensitivity]. 2003 Jan 37