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

1. A process is described for the chemical attachment of an enzyme to the surface of a polystyrene matrix. 2. By this process yeast beta-fructofuranosidase was chemically attached to the surface of both polystyrene beads and polystyrene tubes. 3. The kinetics of sucrose hydrolysis by beta-fructofuranosidase and polystyrene-supported beta-fructofuranosidase were compared. 4. The pH-activity curve of the polystyrene-supported enzyme shows a marked difference from that of the free enzyme in solution. 5. The inhibitor dissociation constant with respect to tris is increased, whereas the inhibitor dissociation constant with respect to aniline is decreased when the enzyme is attached to polystyrene. 6. Differences between the properties of the bound and free enzyme are discussed in terms of a micro-environmental effect arising from the hydrophobic nature of the polystyrene support.
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PMID:The preparation and properties of yeast beta-fructofuranosidase chemically attached to polystyrene. 549 26

beta-Fructofuranosidase [EC 3.2.1.26] in Clostridium perfringens was induced in the presence of sucrose and suppressed in the presence of glucose or maltose. The enzyme seems to be present in protoplasm in a soluble state. The beta-fructofuranosidase from C. perfringens cells grown on sucrose was purified by ammonium sulfate precipitation. DEAE-cellulose chromatography, Sephadex G-150 gel filtration, and hydroxylapatite chromatography to a homogeneous state. The molecular weight was 37,000 by gel filtration using Sephadex G-150 and by SDS-polyacrylamide gel electrophoresis. The amino acid composition is not much different from those of other microorganisms, but the Glx content was a little higher. The enzyme was inhibited by heavy metals, such as Hg2+, Cu2+, and Ag+, as well as pCMB; the activity was restored by incubating with mercaptoethanol. Fructose and amines including Tris and aniline had inhibitory effects.
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PMID:Purification and properties of beta-fructofuranosidase from Clostridium perfringens. 914 17