Hydrophobic Properties of NAD Glycohydrolase from Neurospora Crassa Conidia and Interaction with Dioxane
作者： Mario Pace , Dario Agnellini , Guido Lippoli , Robert L. Berger
DOI: 10.1007/978-1-4419-8632-0_51
关键词: Specific activity 、 Genetics 、 Enzyme 、 Monomer 、 Biology 、 Moiety 、 Dimer 、 Carboxylic acid 、 Stereochemistry 、 Neurospora crassa 、 Hydrophobic effect
摘要: NAD glycohydrolase (NADase, EC 3.2.2.5) from Neurospora crassa conidia shows marked hydrophobic properties which are related to the self inhibition of enzyme. Both aliphatic amines and carboxylic acids able inhibit noncompetitively catalytic activity enzyme depends on non-polar moiety substances. Also dioxane is an inhibitor even though it apparently increases specific This effect can be explained by fact that NADase present as a dimer when concentrated or at high temperature, binds breaking bonds in dimeric yielding most active monomeric form only slightly inhibited organic solvent.
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