Repository of Research and Investigative Information

Repository of Research and Investigative Information

Ilam University of Medical Sciences

Amine oxidase from lentil seedlings: Energetic domains and effect of temperature on activity

Wed Sep 28 18:55:09 2022

(2001) Amine oxidase from lentil seedlings: Energetic domains and effect of temperature on activity. Journal of Protein Chemistry. pp. 405-411. ISSN 02778033 (ISSN)

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Official URL: https://www.scopus.com/inward/record.uri?eid=2-s2....

Abstract

Copper/TPQ amine oxidases from mammalian and plant sources have shown many differences in substrate specificity and molecular properties. In this work the activity of lentil seedling amine oxidase was followed at various temperatures in 100 mM potassium phosphate buffer, pH 7, using benzylamine as substrate. The discontinuous Arrhenius plot of lentil amine oxidase showed two distinct phases with a jump between them. Thermal denaturation of the enzyme, using differential scanning calorimetry under the same experimental conditions, showed a transition at the same temperature ranges in the absence of substrate, indicating the occurrence of conformational changes, with an enthalpy change of about 175.9 kJ/mole. The temperature-induced changes of the activity of lentil amine oxidase are compared with those of bovine serum amine oxidase (taken from the literature).

Item Type: Article
Creators:
CreatorsEmail
Moosavi-Nejad, S. Z.UNSPECIFIED
Rezaei-Tavirani, M.UNSPECIFIED
Padiglia, A.UNSPECIFIED
Floris, G.UNSPECIFIED
Moosavi-Movahedi, A. A.UNSPECIFIED
Keywords: Amine oxidases comparison Copper-containing amine oxidase Differential scanning calorimetry Lentil seedling amine oxidase (flavin containing) resorcinol article catalysis conformational transition crystal structure deamination enthalpy enzyme active site enzyme specificity enzyme substrate human plant seed protein domain temperature dependence Amine Oxidase (Copper-Containing) Amino Acid Sequence Calorimetry Energy Metabolism Enzyme Activation Lens Plant Molecular Sequence Data Sequence Alignment Temperature Arrhenius Bovinae Lens culinaris Mammalia
Divisions:
Page Range: pp. 405-411
Journal or Publication Title: Journal of Protein Chemistry
Journal Index: Scopus
Volume: 20
Number: 5
Identification Number: https://doi.org/10.1023/A:1012284821503
ISSN: 02778033 (ISSN)
Depositing User: مهندس مهدی شریفی
URI: http://eprints.medilam.ac.ir/id/eprint/1697

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