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Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase
( S. Zahra Moosavi Nejad ),( Ali Akbar Moosavi Movahedi ),( Mostafa Rezaei Tavirani ),( Giovanni Floris ),( Rosaria Medda ) 생화학분자생물학회 2003 BMB Reports Vol.36 No.2
The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between 47-60℃. The thermal inactivation curves were not linear at 52 and 57℃; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the conformational lock pertaining theory to oligomeric enzyme. The conformational lock caused two additional dimeric forms of the enzyme when the temperature increased to 50℃. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form conformational lock, conferring a structural tolerance to the enzyme against heat stress.
Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase
Moosavi-Nejad, S. Zahra,Moosavi-Movahedi, Ali-Akbar,Rezaei-Tavirani, Mostafa,Floris, Giovanni,Medda, Rosaria Korean Society for Biochemistry and Molecular Biol 2003 Journal of biochemistry and molecular biology Vol.36 No.2
The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between $47-60^{\circ}C$. The thermal inactivation curves were not linear at 52 and $57^{\circ}C$; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the "conformational lock" pertaining theory to oligomeric enzyme. The "conformational lock" caused two additional dimeric forms of the enzyme when the temperature increased to $57^{\circ}C$. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form "conformational lock," conferring a structural tolerance to the enzyme against heat stress.