muramidase and quinone

muramidase has been researched along with quinone* in 2 studies

Other Studies

2 other study(ies) available for muramidase and quinone

ArticleYear
Inhibition of amyloid fibrillation of lysozyme by phenolic compounds involves quinoprotein formation.
    FEBS letters, 2012, Nov-16, Volume: 586, Issue:22

    Numerous phenolic compounds have been reported to have an inhibitory role on amyloid formation of proteins. The present study, utilizing lysozyme as a model system, examined the anti-amyloidogenic effects of phenol and three diphenol epimers. The results indicated that catechol and hydroquinone dose-dependently inhibited lysozyme fibrillation and covalently bound to the peptide chains to form quinoproteins, showing a similar effect to benzoquinone. In contrast, phenol and resorcinol did not modify the peptide with a quinone moiety, showing no effect on lysozyme fibrillation. We suggest that quinone intermediates are the active form for a phenolic compound to inhibit lysozyme fibrillation. The modification of lysozyme with quinone moieties alters the interacting forces between peptide chains and consequently interrupts the process of lysozyme fibrillation.

    Topics: Amyloid; Benzoquinones; Catechols; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Hydroquinones; Kinetics; Microscopy, Electron, Transmission; Molecular Structure; Muramidase; Phenols; Protein Binding; Resorcinols

2012
Inhibitory effects of plant phenols on the activity of selected enzymes.
    Journal of agricultural and food chemistry, 2002, Jun-05, Volume: 50, Issue:12

    Selected enzymes (alpha-amylase, trypsin, and lysozyme) were allowed to react with some simple phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, m-, o-, and p-dihydroxybenzenes, quinic acid, and p-benzoquinone). The derivatized enzymes obtained were characterized in terms of their activity. In vitro experiments showed that the enzymatic activity of the derivatives was adversely affected. This enzyme inhibition depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The decrease in the activity was accompanied by a reduction in the amount of free amino and thiol groups, as well as tryptophan residues, which resulted from the covalent attachment of the phenolic and related compounds to these reactive nucleophilic sites in the enzymes. The enzyme inhibition correlates well with the blocking of the mentioned amino acid side chains.

    Topics: alpha-Amylases; Benzoquinones; Caffeic Acids; Chlorogenic Acid; Coumaric Acids; Enzyme Inhibitors; Gallic Acid; Hydroquinones; Muramidase; Phenols; Plants; Quinic Acid; Trypsin; Trypsin Inhibitors

2002