Effects of pH on the activity and structure of choline oxidase from Alcaligenes species. | Zendy

Azadeh Hekmat | Zendy; Ali Akbar Saboury | Zendy; Ali Akbar Moosavi–Movahedi | Zendy; Hedayatollah Ghourchian | Zendy; Faizan Ahmad | Zendy

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Effects of pH on the activity and structure of choline oxidase from Alcaligenes species.

Author(s) -

Azadeh Hekmat,

Ali Akbar Saboury,

Ali Akbar Moosavi–Movahedi,

Hedayatollah Ghourchian,

Faizan Ahmad

Publication year - 2008

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2008_3061

Subject(s) - chemistry , choline oxidase , enthalpy , enzyme , arrhenius equation , oxidase test , choline , active site , reaction rate constant , conformational change , biochemistry , stereochemistry , activation energy , kinetics , thermodynamics , acetylcholinesterase , physics , quantum mechanics

A reversible effect of pH on the ionization of amino-acid residues at the active center of choline oxidase was observed near the optimum pH (8). Inactivation of choline oxidase took place in the pH ranges 3-6 and 9-11, in which irreversible changes in the structure occur leading to the enzyme inactivation. The first order rate constants of the enzyme's inactivation at various pH values were estimated for the irreversible changes. The Arrhenius analysis revealed no significant changes in the activation enthalpy, while an increase in the activation entropy reflected an increase in the conformational freedom.

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