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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)

Data obtained concerning the carbohydrate moieties of the glycoenzyme invertase (EC 3.2.1.26, beta-D-fructofuranoside fructohydrolase) from Neurospora crassa were consistent with a linkage of some carbohydrate chains by O-glycosidic bonds to serine and threonine residues; the possibility of N-glycosylamine linkage of some of the carbohydrate to the amide group of asparagine is also indicated. The invertase was remarkably stable on storage at low temperatures. Oxidation of the carbohydrate residues in the enzyme by sodium periodate markedly affected the heat-stability of the enzyme. It is suggested that the carbohydrate moieties function as stabilizers of the tertiary structure of the glycoenzyme.
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PMID:The role of carbohydrate in the glycoenzyme invertase of Neurospora crassa. 19 81

Pea leaves were illuminated in air containing 150 or 1000p.p.m. of 14CO2 for various times. Alternatively, segments of wheat leaves were supplied with [3-14C]serine for 40 min in the light in air with 145, 326 or 944p.p.m. of 12CO2. Sucrose was extracted from the leaf material, hydrolysed with invertase, and 14C in the pairs of carbon atoms C-3+C-4, C-2+C-5 and C-1+C-6 in the glucose moiety was measured. The results obtained after metabolism of 14CO2 were consistent with the operation of the photosynthetic carbon-reduction cycle; the effects of CO2 concentration on distribution of 14C in the carbon chain of glucose after metabolism of [3-14C]serine is more easily explained by metabolism through the glycollate pathway than by the carbon-reduction cycle.
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PMID:Intramolecular labelling of sucrose made by leaves from [14C)carbon dioxide or [3-14C]serine. 65 73

The TUP1 and CYC8 (= SSN6) genes of Saccharomyces cerevisiae play a major role in glucose repression. Mutations in either TUP1 or CYC8 eliminate or reduce glucose repression of many repressible genes and induce other phenotypes, including flocculence, failure to sporulate, and sterility of MAT alpha cells. The TUP1 gene was isolated in a screen for genes that regulate mating type (V.L. MacKay, Methods Enzymol. 101:325-343, 1983). We found that a 3.5-kb restriction fragment was sufficient for complete complementation of tup1-100. The gene was further localized by insertional mutagenesis and RNA mapping. Sequence analysis of 2.9 kb of DNA including TUP1 revealed only one long open reading frame which predicts a protein of molecular weight 78,221. The predicted protein is rich in serine, threonine, and glutamine. In the carboxyl region there are six repeats of a pattern of about 43 amino acids. This same pattern of conserved residues is seen in the beta subunit of transducin and the yeast CDC4 gene product. Insertion and deletion mutants are viable, with the same range of phenotypes as for point mutants. Deletions of the 3' end of the coding region produced the same mutant phenotypes as did total deletions, suggesting that the C terminus is critical for TUP1 function. Strains with deletions in both the CYC8 and TUP1 genes are viable, with phenotypes similar to those of strains with a single deletion. A deletion mutation of TUP1 was able to suppress the snf1 mutation block on expression of the SUC2 gene encoding invertase.
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PMID:Characterization of TUP1, a mediator of glucose repression in Saccharomyces cerevisiae. 224 69

Site-specific recombination requires conserved DNA sequences specific to each system, and system-specific proteins that recognize specific DNA sequences. The site-specific recombinases seem to fall into at least two families, based on their protein structure and chemistry of strand breakage. One of these is the resolvase-invertase family, members of which seem to form a serine-phosphate linkage with DNA. Members of the other family, called the integrase family, contain a conserved tyrosine residue that forms a covalent linkage with the 3'-phosphate of DNA at the site of recombination. Structural comparison of integrases shows that these proteins share a highly conserved 40-residue motif. V-(D)-J recombination of the immunoglobulin gene requires conserved recombination signal sequences (RS) of a heptamer CACTGTG and a T-rich nonamer GGTTTTTGT, which are separated by a spacer sequence of either 12 or 23 bases We have recently purified, almost to homogeneity, a protein that specifically binds to the immunoglobulin J kappa RS containing the 23-base-pair spacer sequence. By synthesizing probes on the basis of partial amino-acid sequences of the purified protein, we have now isolated and characterized the complementary DNA of this protein. The amino-acid sequence deduced from the cDNA sequence reveals that the J kappa RS-binding protein has a sequence similar to the 40-residue motif of integrases of phages, bacteria and yeast, indicating that this protein could be involved in V-(D)-J recombination as a recombinase.
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PMID:A protein binding to the J kappa recombination sequence of immunoglobulin genes contains a sequence related to the integrase motif. 255 44

Aging is associated with changes in the intestinal uptake of nutrients. This study was undertaken to determine whether the morphology, enzyme markers and the lipid content of the intestinal brush border membrane (BBM) was influenced by aging. There was an increase in the height of the jejunal villi and number of cells/villus, resulting in an age-related increase in the jejunal villus and mucosal surface area in young as compared with weanling rabbits. In mature 1-year-old animals, there was a decline in villus height, number of cells/villus, and mucosal surface area, so that the jejunal characteristics of the mature animals resembled those of the weanling rabbits. In the ileum, aging was associated with an increase (weanling vs. young), then a decrease (young vs. mature) in the height of the villi, and the number of cells/villus. Aging had no effect on the size of the villus cells. At all ages there was a direct positive relationship between the height of the villi and the mucosal surface area, and between villus surface area and sucrase activity. An established technique was used to purify rabbit BBM and to measure the BBM content of enzyme markers and lipids in weanling, young and mature animals. Both the BBM sucrase (S) and alkaline phosphatase (AP) increased in young as compared with weanling rabbits, and the ratio of AP/S remained unchanged. The S remained high in mature rabbits, but AP declined, so that AP/S fell. There was a positive linear correlation between S and villus surface area. In weanling rabbits, the total BBM phospholipid content and the ratio of total phospholipid/total cholesterol were lower in the ileum than in the jejunum. In the jejunal BBM of young animals, there was more total free fatty acids and cholesterol ester than in the weanling jejunum. The jejunal BBM total phospholipids and total cholesterol were higher in the mature than in the weanling animal jejunum when expressed as nmoles/mg protein, but the ratio of total phospholipid/total cholesterol was unaffected by aging. The greatest percentage of jejunal BBM phospholipid was comprised of lecithin and phosphatidyl ethanolamine. The increased BBM total phospholipid content in mature animals was associated with a higher amount and lower proportion of lecithin, but a higher proportion of sphingomyelin and phosphatidyl serine.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Intestinal morphology, marker enzymes and lipid content of brush border membranes from rabbit jejunum and ileum: effect of aging. 299 64

The DNA invertase Gin encoded by bacteriophage Mu catalyses efficient site-specific recombination between inverted repeat sequences (IR) in vivo and in vitro in the presence of the host factor FIS and the recombinational enhancer. We demonstrate that Gin alone is able to introduce single strand breaks into duplex DNA fragments which contain the IR sequence. Strand cleavage is site-specific and can occur on either strand within the IR. Cleaved molecules contain Gin covalently attached to DNA. The covalent complex is formed through linkage of Gin to the 5' DNA phosphate at the site of the break via a phosphoserine. Extensive site-directed mutational analysis showed that all mutants altered at serine position 9 were completely recombination deficient in vivo and in vitro. The mutant proteins bind to DNA but lack topoisomerase activity and are unable to introduce nicks. This holds true even for a conservative amino acid substitution at position 9. We conclude that serine at position 9 is part of the catalytic domain of Gin. The intriguing finding that the DNA invertase Gin has the same catalytic center as the DNA resolvases that promote deletions without recombinational enhancer and host factor FIS is discussed.
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PMID:The DNA invertase Gin of phage Mu: formation of a covalent complex with DNA via a phosphoserine at amino acid position 9. 304 82

The complete primary structure (1827 amino acids) of rabbit intestinal pro-sucrase-isomaltase (pro-SI) was deduced from the sequence of a nearly full-length cDNA. Pro-SI is anchored in the membrane by a single 20 amino acid segment spanning the bilayer only once. The amino-terminal, cytoplasmic domain consists of 12 amino acids and is not preceded by a cleaved leader sequence. This suggests a dual role for the membrane-spanning segment as an uncleaved signal for membrane insertion. This is followed by a 22 residue serine/threonine-rich, probably glycosylated, stretch, presumably forming the stalk on which the globular, catalytic domains are directed into the intestinal lumen. Following this is a high degree of homology between the isomaltase and sucrase portions (41% amino acid identity), indicating that pro-SI evolved by partial gene duplication.
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PMID:The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. 375 79

Isocitrate lyase is a key catalyst of the glyoxylate cycle. A feature of the enzyme from higher plants is the high instability, that causes innumerable problems in working for characterization of the enzyme. The present communication demonstrates that the optimal conditions for the storage of isocitrate lyase from Pinus pinea are: the use of a low temperature (possibly below -20 degrees C), the realization of a high endogenous protein concentration of the enzyme preparations, or, above all when long storage conservation is necessary, the preservation of the enzyme in dried form (acetone precipitation), under vacuum at 4 degrees C. The data reported in this paper seem to exclude, in the above studied conditions, a role for serine proteases in the destabilization of the enzyme. The thiol compounds are not determinant and no effect is obtained by adding exogenous proteins (serum albumin, beta-fructosidase).
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PMID:On the stability of isocitrate lyase from Pinus pinea. 712 56

Site-specific recombinases of the resolvase and DNA invertase family all contain a tyrosine residue close to the N-terminus, and four residues away from a serine that has been implicated in catalysis of DNA strand breakage and reunion. To examine the role of this tyrosine in recombination, we have constructed a mutant of gamma delta resolvase in which the tyrosine (residue 6) is replaced by phenylalanine. Characterization of the Y6F mutant protein in vitro indicated that although it was highly defective in recombination, it could cleave DNA at the cross-over site, form a covalent resolvase-DNA complex and rejoin the cleaved cross-over site (usually restoring the parental site). These data rule out a direct role of the Tyr-6 hydroxyl as the nucleophile in the DNA cleavage reaction and strengthen the conclusion that this nucleophile is the nearby invariant serine residue, Ser-10. We conclude that Tyr-6 is essential for fully co-ordinated strand cleavage and exchange, but is dispensable for individual strand cleavage and religation reactions.
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PMID:The tyrosine-6 hydroxyl of gamma delta resolvase is not required for the DNA cleavage and rejoining reactions. 759 88

Autophagocytosis is a starvation-induced process, carrying proteins destined for degradation to the lysosome. In the yeast Saccharomyces cerevisiae, the autophagic process is visualized by the appearance of autophagic vesicles in the vacuoles of proteinase yscB-deficient strains during starvation. aut3-1 mutant cells which exhibit a block in the autophagic process have been isolated previously. By using the drastically reduced sporulation frequency of homozygous aut3-1 diploid cells, the AUT3 gene was cloned by complementation. The Aut3 protein consists of 897 amino acids. The amino-terminal part of the protein shows significant homologies to serine/threonine kinases. aut3 null mutant cells are fully viable on rich media but show a reduced survival rate upon starvation. They are unable to accumulate autophagic vesicles in the vacuole during starvation. Starvation-induced vacuolar protein breakdown is almost completely impaired in aut3-deficient cells. Vacuolar morphology and acidification are not influenced in aut3-deficient cells. Also, secretion of invertase, endocytic uptake of Lucifer Yellow, and vacuolar protein sorting appear wild type like in aut3-deficient cells, suggesting autophagocytosis as a novel route for the transport of proteins from the cytosol to the vacuole. By using a fusion of Aut3p with green-fluorescent protein, Aut3p was localized to the cytosol.
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PMID:AUT3, a serine/threonine kinase gene, is essential for autophagocytosis in Saccharomyces cerevisiae. 919 Aug 2


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