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:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The separation by polyacrylamide gel electrophoresis and subsequent enzymatic analysis of the components of the guinea pig intestinal brush border membrane revealed the presence of three enzyme complexes: maltase-glucoamylase, maltase-sucrase-glucoamylase and maltase-sucrase. Additional bands possessing lactase, trehalase and alkaline phosphatase activity were identified but no phlorizin hydrolase or palatinase was detectable. After exposure to strong dissociating conditions the bands possessing enzymatic activity were either absent or greatly reduced in intensity.
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PMID:Glycosidases of the guinea pig brush border membrane. 86 Dec 25

Starch digestion and absorption is augmented appreciably by physical processing of grain or legume and by heating to 100 degrees C for several minutes before its ingestion. Starch, a polysaccharide composed of alpha 1,4-linked glucose units (amylose) and alpha 1,4-1,6-linked branched structure (amylopectin), is cleaved in the duodenal cavity by secreted pancreatic alpha-amylase to a disaccharide (maltose), trisaccharide (maltotriose), and branched alpha-dextrins. These final oligosaccharides are hydrolyzed efficiently by complimentary action of three integral brush border enzymes at the intestinal surface: glucoamylase (maltase-glucoamylase, amyloglucosidase), sucrase (maltase-sucrase) and alpha-dextrinase (isomaltase). The final monosaccharide glucose product is then cotransported into the enterocyte along with Na+ by a specific brush border 75-kDa transport protein in the rate-limiting step for overall starch assimilation. By virtue of this sequential luminal and membrane digestion followed by glucose transport, starch is assimilated in a very efficient manner in nonruminants.
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PMID:Starch digestion and absorption in nonruminants. 172 68

We have described the methods used for studying the biosynthesis and the post-translational processing of sucrase-isomaltase (SI), lactase-phlorizin hydrolase (LPH) and maltase-glucoamylase (MGA) in human small intestinal mucosa. Our results are discussed in the context of findings by other researchers. A surprising finding coming out of all these studies is that SI, LPH and MGA are structurally quite different. SI and LPH are both synthesized as large molecular weight precursors which are proteolytically processed to the mature enzymes. In the case of SI, this processing occurs after insertion of the precursor into the brush border membrane and is catalysed by pancreatic proteases; the mature form consists of the two subunits sucrase and isomaltase, the latter containing an N-terminal peptide anchor. Proteolytic processing of the LPH-precursor occurs intracellularly, yielding a mature enzyme in the form of a two active site polypeptide which is anchored via a C-terminal peptide. The role of the large cleaved propolypeptide of LPH is not yet known. MGA is the largest of the three disaccharidases, having a molecular weight of greater than 300 kDa. No proteolytic processing seems to be taking place during biogenesis of MGA in human mucosa, and the mode of attachment to the membrane is unknown at present. The application of the methods described to the investigation of congenital sucrase-isomaltase deficiency (CSID) and lactase restriction in adults is presented and differences between CSID and LPH restriction are discussed.
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PMID:Molecular aspects of disaccharidase deficiencies. 211 33

Adult rats that were maintained on a low-carbohydrate intake showed rapid increase in the activities of sucrase, maltase, and lactase along the length of the small intestine when they were fed a high-starch diet. In the present study, we have identified these activity increases, and showed that they reflect proportional accumulations in enzyme-protein of sucrase-isomaltase (EC 3.2.1.10, 3.2.1.48), maltase-glucoamylase (EC 3.2.1.20), and neutral lactase (EC 3.2.1.23). It was determined that each of these enzymes exists in adult rat intestine in single immunoreactive form and accounts as a group for all sucrase, cellobiase, and most maltase and lactase activities. Dietary change from low to high carbohydrate (starch) resulted in an increase in [3H]leucine accumulation in each of the enzymes, without a change in the amount of label accumulation in total intestinal proteins. The increase in label accumulation in the brush-border carbohydrase pools was matched generally by proportional elevation in the pool concentrations of sucrase-isomaltase and lactase but not maltase. These studies suggest that the elevation of intestinal carbohydrase concentrations induced by high-carbohydrate feeding may involve selective stimulation of their synthesis.
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PMID:Nature of elevated rat intestinal carbohydrase activities after high-carbohydrate diet feeding. 241 70

Adult rats when fed a high carbohydrate diet of 70% sucrose or glucose for 24 h following a 4-day fast showed increased concentrations of intestinal sucrase-isomaltase (EC 3.2.1.48, EC 3.2.1.10) and maltase-glucoamylase (EC 3.2.1.20) but not lactase-phlorizin hydrolase (EC 3.2.1.23, EC 3.2.1.62). The concentration increases of these enzymes were accompanied by corresponding acceleration of their synthesis rates. Contrary to earlier studies by others, suggesting that upper villus cells in the fasted intestine are unresponsive to stimulation of sucrase activity by refeeding a high-sucrose diet, the concentration increases of both sucrase-isomaltase and maltase-glucoamylase were seen to occur in cells all along the length of the villus column. The earlier studies differed from the present study by basing enzyme assays relative to protein rather than the DNA content of villus cell fractions. We have shown that villus cells increase their protein content severalfold while migrating to villus tip, providing the basis for the difference between earlier and the present findings. Further evidence that stimulation of sucrase-isomaltase and maltase-glucoamylase by high carbohydrate is not restricted to the crypt and lower villus region was obtained by the finding that their synthesis rates appeared to be equally stimulated along the length of the villus column.
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PMID:Dietary CHO and stimulation of carbohydrases along villus column of fasted rat jejunum. 249 55

1. Trehalase, sucrase-isomaltase and maltase-glucoamylase are three integral glycoproteins of the brush border membranes of the enterocytes. On the basis of a comparative study on alpha-glycosidase activities (sucrase, isomaltase, maltase, glucoamylase and trehalase) associated to these glycoproteins during neonatal development, mammals could be basically divided into three groups. 2. In rodents and rabbit alpha-glycosidase activities are low or undetectable during the suckling period and increase to adult levels during the weaning period. In cat, dog and the primates examined, alpha-glycosidase activities are well or fully developed at birth. 3. In ruminants and pinnipedia alpha-glycosidases are low or absent throughout life. 4. During the suckling period of rat, mouse and rabbit, glucocorticoids trigger a premature and dramatic increase of all alpha-glycosidases. 5. On the contrary, alpha-glycosidases development during the weaning period appears to be independent of glucocorticoids. Neither hypophysectomy nor adrenalectomy prevent the development of alpha-glycosidases; only the rate of increase is reduced. 6. Transplantations of intestinal isografts either in adult or suckling animal, have shown that (1) no systemic factor inhibits the expression of alpha-glycosidase, (2) alpha-glycosidases induction is neither triggered by luminal alimentary substances, nor by hormones, (3) alpha-glycosidase development is controlled by an intrinsic ontogenic program. 7. The use of an antiglucocorticoid failed to inhibit the spontaneous development of alpha-glycosidase activities. 8. The increase of maltase and sucrase activities triggered by glucocorticoids is associated with an increase of the concentration of two glycoproteins in the microvillous membrane: sucrase-isomaltase and maltase-glucoamylase. 9. After administration of glucocorticoids the increase of maltase, sucrase and trehalase is strongly inhibited by actinomycin-D and the increase of sucrase activity is associated with a parallel increase of sucrase-isomaltase mRNA. Transcription is most likely the primary site of control of alpha-glycosidase biosynthesis. 10. In the crypt cells, alpha-glycosidases biosynthesis appears to be triggered by a receptor-mediated glucocorticoid interaction. 11. The enterocytes synthesize more alpha-glycosidase molecules as they travel to the tip of the villi. 12. The simultaneous, biosynthesis of sucrase-isomaltase and maltase-glucoamylase triggered by glucocorticoids, as well as their simultaneous normal development suggest that they may be subjected to related control mechanisms. 13. It is suggested that sucrase-isomaltase and maltase-glucoamylase might have arisen by several cycles of partial gene duplication of an ancestor gene coding for a single site maltase-isomaltase; subsequent mutation would have transformed isomaltase into sucrase or glucoamylase.
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PMID:Brush border membrane sucrase-isomaltase, maltase-glucoamylase and trehalase in mammals. Comparative development, effects of glucocorticoids, molecular mechanisms, and phylogenetic implications. 251 62

Small intestinal biopsies from nine patients with sucrase-isomaltase deficiency (sucrose-intolerance) were analyzed. All patients lacked sucrase activity and three patients had a residual isomaltase activity and a corresponding isomaltase precipitate following immunoelectrophoresis. By polyacrylamide gel electrophoresis in sodium dodecyl sulfate followed by immunoblotting the residual isomaltase appeared as a single polypeptide with molecular weight of approximately 145,000. Maltase-glucoamylase in the biopsies was specifically quantitated by crossed immunoelectrophoresis. One of the patients had an almost total deficiency of maltase-glucoamylase in the biopsy, three patients had a normal amount of maltase-glucoamylase, and five patients constituted an intermediary group. These results indicate that some of the sucrase-isomaltase deficient patients also have a more or less pronounced deficiency of maltase-glucoamylase. The patients constitute an even more heterogeneous group than earlier suggested and should be classified by the amount not only of sucrase and isomaltase but also of maltase-glucoamylase.
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PMID:Maltase-glucoamylase and residual isomaltase in sucrose intolerant patients. 308 47

Chicken intestinal sucrase-isomaltase and maltase-glucoamylase have been isolated in their intact form by detergent solubilization and characterized as to their subunit composition and mode of anchoring in the brush-border membrane. Both are heterodimeric enzyme complexes composed of two subunits each of approximately 140 and 130 kDa. Contrary to the mammalian sucrase-isomaltase, chicken isomaltase was identified as the smaller of the two subunits. As was shown by hydrophobic labeling, only one of the two subunits in each heterodimer is anchored in the bilayer, the smaller 130 kDa isomaltase subunit of the sucrase-isomaltase complex, and the larger 140 kDa subunit of the maltase-glucoamylase complex. Both preparations contain a high-molecular weight polypeptide of approximately 250 kDa which in the case of sucrase-isomaltase could be identified by peptide mapping as a single-chain precursor not (yet) proteolytically processed to the final heterodimer. These first data on the mode of membrane anchoring of non-mammalian glycosidases indicate that they are synthesized, inserted into the membrane, and processed in ways similar to the mammalian enzymes. The fundamental unity between avian and mammalian sucrase-isomaltases suggests that the partial gene duplication of an ancestral isomaltase gene and the subsequent mutation of one of the active sites resulting in pro-sucrase-isomaltase has occurred prior to the separation of mammals from reptiles, i.e. more than 300 million years ago.
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PMID:The mode of anchoring and precursor forms of sucrase-isomaltase and maltase-glucoamylase in chicken intestinal brush-border membrane. Phylogenetic implications. 309 40

Structural changes have been studied during the life cycles of three glycosidases: sucrase-isomaltase (EC 3.2.48-10), lactase-phlorizin hydrolase (EC 3.2.1.23-62), maltase-glucoamylase (EC 3.2.1.20); and three peptidases: aminopeptidase A (EC 3.4.11.7), aminopeptidase N (EC 3.4.11.2) and dipeptidyl peptidase IV (EC 3.4.14.5). The final forms of the enzymes can be divided into at least two groups: the sucrase-isomaltase type, characterized as dimers, which are asymmetric in their hydrophilic parts, have two types of active site and anchor only on one subunit; and the aminopeptidase N type, characterized as dimers, which are symmetric in their hydrophilic part, have only one type of active site and anchor on both subunits. These enzymes are likely to be synthesized on rough endoplasmic reticulum and simultaneously glycosylated into endoglycosidase H-sensitive forms. They are later reglycosylated to endoglycosidase H-resistant forms, which have relative molecular masses similar to the final forms. Enzymes of the sucrase-isomaltase type seem to be synthesized with a polypeptide-chain length corresponding to the sum of both subunits, whereas enzymes of the aminopeptidase N type seem to be synthesized with a polypeptide-chain length corresponding to the constituent subunits themselves. Not much is known about the catabolism of these enzymes. The enzyme activities and the amounts of enzyme protein decrease at the top of the villi, probably due to release into the lumen. The subunits of aminopeptidase N are cleaved by pancreatic proteases to smaller peptides, and sucrase-isomaltase may lose its sucrase polypeptide, while both enzymes remain bound to the membrane.
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PMID:Structure of microvillar enzymes in different phases of their life cycles. 613 6

Sucrase-isomaltase (S-I) and maltase-glucoamylase (M-G) of the brush border have been purified to electrophoretic homogeneity from the pigeon small intestine. Heat-inactivated enzymes of crude homogenates of the pigeon intestinal mucosa, papain-solubilized enzymes and those obtained after chromatographic fractionation behaved in an identical manner. Depending on their sensitivity to heat treatment, the disaccharidases were identified to consist of two maltases; one, the heat-labile maltase, and the other, the heat-stable maltase. Sucrase and isomaltase constituted the thermolabile maltase and could be distinguished from each other. Maltase and glucoamylase formed the thermostable maltase the activities of which however, remained inseparable. Based on these results and in accordance with the nomenclature suggested by Dahlqvist & Telenius (1969), the pigeon intestinal disaccharidases were classified as follows: Maltase Ia = isomaltase, Maltase Ib = sucrase, and Maltase II = glucoamylase. DEAE-Cellulose chromatography did not resolve the two enzyme complexes but gel filtration of the active fractions recovered from the former step, resulted in their separation into two distinct peaks. Sucrase, isomaltase and a part of the maltase activity were recovered in the first peak which eluted close to the void volume. Glucoamylase and the remaining maltase activity were recovered in the second peak which appeared to have been retarded on the column because they were eluted much more slowly. The S-I and M-G complexes have an apparent molecular weight of 195 kd and 209 kd as determined by their gel-filtration pattern on Sepharose 6B. S-I hydrolysed alpha-glucosides such as maltose, sucrose and palatinose with a Km of 3.12 mM, 8 mM and 8.36 mM respectively and did not attack starch or dextran. In contrast, M-G catalysed the hydrolysis of starch, amylose and maltose with a Km of 3.12 mM, 7.59 mM and 3.52 mM respectively, and had no action on sucrose or palatinose. Both S-I and M-G were glycoproteins, and were inhibited by Ag+, Hg2+ and Tris but not by p-hydroxymercuribenzoate, iodoacetamide or imidazole. Na+ on the other hand activated both the enzyme complexes by about 20-25%. It is suggested that the molecular and catalytic properties of intestinal disaccharidases of pigeons do not differ considerably from those of Mammals.
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PMID:Studies on the intestinal disaccharidases of the pigeon. III. Separation, purification and properties of sucrase-isomaltase and maltase-glucoamylase. 620 6


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