Thermal Dissection of Lentil Seedling Amine Oxidase Domains by Differential Scanning Calorimetry | Zendy

Ali Akbar Moosavi–Movahedi | Zendy; Mojtaba Amani | Zendy; Zahra Moosavi-Nejad | Zendy; Sedigheh Hashemnia | Zendy; Faizan Ahmad | Zendy; Giovanni Floris | Zendy; Anna Mura | Zendy; Mostafa RezaeiTavirani | Zendy; G. H. HAKIMELAHI | Zendy; Ali Akbar Saboury | Zendy; Reza Yousefi | Zendy

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Thermal Dissection of Lentil Seedling Amine Oxidase Domains by Differential Scanning Calorimetry

Author(s) -

Ali Akbar Moosavi–Movahedi,

Mojtaba Amani,

Zahra Moosavi-Nejad,

Sedigheh Hashemnia,

Faizan Ahmad,

Giovanni Floris,

Anna Mura,

Mostafa RezaeiTavirani,

G. H. HAKIMELAHI,

Ali Akbar Saboury,

Reza Yousefi

Publication year - 2007

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.70039

Subject(s) - differential scanning calorimetry , chemistry , isothermal titration calorimetry , thermal stability , enzyme , active site , amine gas treating , moiety , biochemistry , stereochemistry , organic chemistry , physics , thermodynamics

The relationships between the structural and energetic domains of lentil seedling amine oxidase (LSAO) were investigated using modifiers that target the active site and the carbohydrate moiety of the enzyme. An irreversible inhibitor, aminoguanidine, specifically modified the active site of the lentil enzyme, whereas sodium metaperiodate cleaves carbohydrate moieties covalently bound to the native enzyme. Differential scanning calorimetry (DSC) measurements were made on the modified LSAOs. Deconvolution of the reversible thermal DSC profiles of the modified enzyme gave three subpeaks (energetic domains), each of which was assigned to one of the three structural domains of the native protein. Our results led us to conclude that deglycosylation of LSAO has no effect on thermal stability, whereas binding of the inhibitor imparts more stability to the enzyme.

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