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)

1. The effects on Neurospora crassa invertase (beta-D-fructofuranoside fructohydrolase, EC 3.2.1.26) of a variety of group specific reagnets and other potential inhibitors were determined during a search for an irreversible inhibitor of the enzyme. Aniline, pyridoxal, enzyme substrate and products did not inactivate invertase under reducing conditions. Bromoacetic acid, iodoacetic acid, iodoacetamide, p-chloromercuribenzoate, hydroxylamine and 2-hydroxy-5-nitrobenzyl bromide were also ineffective. Iodine was the only reagent which irreversibly inhibited invertase. 2. Invertase was rapidly inactivated by low concentrations of iodine, indicating specific inhibition. However, the enzyme could not be protected from this inactivation by substrate. It was not reactivated by mercaptoethanol or cysteine. 3. Experiments on the uptake of radioactive iodine demonstrated that invertase is not iodinated under the conditions of iodine inactivation. 4. The sedimentation (S20,w) value of invertase was not altered by iodine inactivation. One-dimensional electrophoresis and finger-printing of tryptic digests revealed no differences between iodine treated and untreated invertase. There was no loss of carbohydrate from this glycoprotein during iodine inactivation. 5. Standard amino acid analyses of iodine-inactivated invertase showed some loss of tyrosine and a trace amount of methionine sulfone. Attempts to demonstrate oxidation of methionine to the sulfone, through modification of the procedure for preparation of samples for analysis, were unsuccessful. However, oxidation of half-cystine was indicated and further loss of tyrosine noted. A hypothesis is advanced that half-cystine is oxidized by iodine to a normally unstable oxidation state which is maintained and protected by its protein invironment and that loss of tyrosine may be an artifact caused by the presence of this residue during acid hydrolysis.
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PMID:Neurospora crassa invertase. A study of amino acids at the active center. 23 50

The superiority of human milk as compared with milk of other origin for the feeding of newborns, term or preterm, can be analysed in terms of biological development related to digestive, metabolic and excretory functions during foetal and postnatal life. The macro- and micro-anatomical developments of the intestine are complete in the 6th foetal month. The brush border and some of its enzymes (saccharase-isomaltase) exist already from the 6th foetal week, whereas other enzymes (lactase and intracellular transport enzymes) appear much later. The major gastric and pancreatic enzymes, as well as the synthesis of biliary acids, do not reach maturity until after birth. Several metabolic functions, e.g. the synthesis of cystine from methionine, of tyrosine from phenylalanine, and of urea from ammonia, are still limited at the time of birth. The capacity for excretion of sodium, the osmotic urinary load, and hydrogen ions is suboptimal, especially in the prematurely born. All these circumstances imply that human milk, with its protective properties, represents optimal adaptation to the needs of the child in the perinatal period.
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PMID:Breast feeding and biological development. 69 1

Experiments on male rats showed that following subcutaneous injection of alloxan in a dose of 15 mg per 100 g of body weight amylolytic, invertase, glycyl-l-tyrosine dipeptidehydrolase activity of the mucosa of the small intestine altered differently. As a result, there occurred a deviation of the enzymatic spectrum from the normal characterized by a sharp increase (with the development of diabetes) of the activity of the carbohydrate hydrolysing enzymes (amylase and invertase) with a simultaneous reduction of the activity of the enzymes participating in protein (dipeptidase) and fat (monglyceridlipase) hydrolysis.
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PMID:[Effect of alloxan diabetes on the enzyme activity of the mucous membrane of the small intestine]. 72 80

1. In native invertase at pH 4.6, 23 out of a total of 34 tryptophyl residues are "exposed" to oxidation with N-bromosuccinimide, the other residues being apparently shielded from the oxidant within the molecule. 2. Oxidation of 5-6 tryptophyl residues/molecule with N-bromosuccinimide is proportional to the complete inactivation of the enzyme, and appears to be specific for indole chromophore only. The ligand binding and fluorescence measurements indicate that the oxidation of native enzyme, up to 50% inhibition, apparently does not change the conformation and topography of enzymes surface. 3. Invertase is inhibited by diazonium-1-H-tetrazole. Since tyrosine residues can be excluded by nitration studies as catalytically unimportant, it appears that a mocification of a single histidyl residue/molecule with diazonium-1-H-tetrazole is sufficient to abolish the enzymic activity. However, the absence of inhibition with diethyl pyrocarbonate indicates that the inhibition with diazonium-1-H-tetrazole may be mediated through steric hindrance or other indirect effects. 4. The absence of inhibition with 2,4-dinitrophenylhydrazine, trinitro benzenesulfonic acid and 5,5'-dithiobis-(2-nitrobenzoate) indicates that the carbonyl groups of the carbohydrate moiety, free amino and -SH groups are not essential for activity.
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PMID:External yeast beta-fructosidase. The role of tryptophyl residues in catalysis. 110 63

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

The inactivation of external yeast invertase by irradiation in dilute aqueous solution has been investigated. The contributions of the individual radical species from water radiolysis to inactivation and amino acid degradation were estimated from the results of experiments in which solutions were saturated with nitrogen, nitrous oxide or oxygen, and on addition of hydroxyl radical scavengers. Under conditions where inactivation by hydroxyl radicals predominates, the rate of inactivation increased with increasing dose, indicating that in the initial stages of the radiolysis the mannose-rich oligosaccharide chains of the glycoprotein protect the polypeptide chain from radical attack. Amino acid analysis of the irradiated external invertase showed that there was significant destruction of tyrosine, phenylalanine, methionine and histidine residues. Destruction of methionine and histidine residues may be responsible for the free radical-induced inactivation of this enzyme.
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PMID:The radiation-induced inactivation of external yeast invertase in dilute aqueous solution. 256 93

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

The enzyme that catalyzed the conversion of human salivary alpha-amylase family A (HSA-A) to family B (HSA-B) was identified. It was partially purified from the precipitate obtained by centrifugation of human saliva at 105,000 x g for 60 min by solubilization with 3[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate and column chromatographies with Sephacryl S-300-HR and hydroxylapatite. The enzyme preparation was practically free from contaminating exoglycosidases and proteases. The enzyme cleaved the N,N'-diacetylchitobiose moiety of the sugar chain of HSA-A, as shown by the isolation of the protein moiety which contained 1 GlcNAc and 1 Fuc residue and the sugar chain (Gal)2(Fuc)1(GlcNAc)2(Man)3(GlcNAc). This enzyme also cleaved the N,N'-diacetylchitobiose moiety of the sugar chain of human transferrin tetraglycopeptide Asn-Tyr-Asn(GlcNAc)2(Man)3(GlcNAc)2(Gal)2-Lys to yield equimolar amounts of peptide Asn-Tyr-Asn(GlcNAc)Lys and sugar chain (Gal)2(GlcNAc)2(Man)3(GlcNAc). The enzyme was identified as an endo-beta-N-acetylglucosaminidase. The enzyme acted on HSA-A with desialylated and defucosylated outer chain moieties of the sugar chains at a similar rate as that of native HSA-A. The enzyme activity was reduced to 13 and 5% using HSA-A with the sugar chains whose outer chain moieties lacked Gal and GlcNAc, respectively, from the nonreducing end. The enzyme also acted on human transferrin, calf fetuin, and asparagine oligosaccharides of transferrin and fetuin. On the other hand, the enzyme did not act on ovalbumin, RNase B, Taka-amylase, yeast invertase, and ovalbumin asparagine oligosaccharides. These results indicate that human salivary endo-beta-N-acetylglucosaminidase is specific for complex type sugar chains and can release the sugar chains from native glycoproteins and glycopeptides regardless of the existence of a Fuc residue on the proximal GlcNAc of the N,N'-diacetylchitobiose core of their sugar chains. The source of the enzyme was epithelial cells peeling from the oral cavity epithelium into saliva. The enzyme was thought to be integrated on the surface of the epithelial cell membrane. This enzyme was named endo-beta-N-acetylglucosaminidase HS. Thus, these studies indicate that the properties of the enzyme are distinct from those of known endo-beta-N-acetylglucosaminidase and endo-beta-N-acetylglucosaminidase HS is a novel endo-beta-N-acetylglucosaminidase.
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PMID:Human salivary endo-beta-N-acetylglucosaminidase HS specific for complex type sugar chains of glycoproteins. 834 Apr 28

Kinetics of the temperature- or pressure-induced denaturation of invertase from Saccharomyces cerevisiae were obtained in the temperature range 45-70 degrees C and in the pressure range 500-650 MPa. The investigation was done by measuring the residual activities after cooling or pressure release and the intrinsic fluorescence of aromatic amino-acids (tyrosine and tryptophan) upon excitation at 277 nm. The residual activity decreased exponentially as a function of time incubation according to a biphasic model either with pressure or temperature, whereas the fluorescence emission indicated a difference between these two parameters. When the enzyme was subjected to thermal treatment, the fluorescence of tyrosine and tryptophan decreased slowly, while after high-pressure treatment, these aromatic residues become more exposed to the aqueous solvent during unfolding, giving rise to a large decrease in fluorescence in the 330-340 nm region. Moreover, in the latter case, an enhancement of light scattering intensity showed changes in protein-protein interactions.
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PMID:Effect of temperature and pressure on yeast invertase stability: a kinetic and conformational study. 859 Jun 48

Numerous studies indicate beneficial effects of glutamine (Gln) in many models of catabolic adult rats. No data were available for aged rats. The effects of oral L-Gln-enriched diet were tested in endotoxemic 24-mo old rats. First, rats received for 7 d (from d0 to d7) an oral diet supplemented with either L-Gln [1g/(kg. d)] or casein (Cas: isonitrogenous supply) prior to lipopolysaccharide (LPS) challenge. The rats were then killed after 24 h food deprivation (from d7 to d8). Endotoxemia induced a catabolic response as shown by muscle glutamine depletion, hyperphenylalaninemia, small bowel atrophy and impaired functionality and bacterial translocation. The Gln-enriched diet did not prevent muscle Gln depletion but significantly (P </= 0.05) enhanced plantaris protein content by 18% compared to the Cas-LPS rats and reduced the plasma phenylalanine-to-tyrosine ratio (1.32 +/- 0.05 vs. 1.54 +/- 0.10, respectively, P </= 0.01). Gut translocation and histomorphology were unaffected by diet. However, Gln pretreatment reduced the fall in sucrase and glucoamylase activities in the ileum, respectively, by 55 and 63% vs. Cas supplementation (P </= 0.05). In a second study, after endotoxin challenge, healthy 24-mo-old rats were then food-deprived for 2 d (from d0 to d2), received a nonpurified diet for 4 d (from d2 to d6), and then Cas or L-Gln-supplemented diet for 7 d (from d6 to d13). No beneficial effects of Gln supplementation were observed except an increase of 50 and 56% in sucrase and glucoamylase activities in the ileum of Gln-treated rats, (P </= 0.01 vs. healthy rats). In conclusion, the effects of L-Gln supplementation in aged endotoxemic rats were limited.
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PMID:Oral administration of a glutamine-enriched diet before or after endotoxin challenge in aged rats has limited effects. 1049 50


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