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

• Autorzy: Hekmat A. , Saboury A.A. , Moosavi-Movahedi A.A. , Ghourchian H. , Ahmad F.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

PL

choline oxidase; glycine-betaine; optimum pH; amino acid residue; ionization; Arrhenius analysis; activation entropy

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2008
• Tom: 55
• Numer: 3
• Strony: 549-557
• Opis fizyczny: p.549-557,fig.,ref.

Twórcy

autor

Hekmat A.

• University of Tehran, PO Box 13145-1384, Tehran, Iran

autor

Saboury A.A.

autor

Moosavi-Movahedi A.A.

autor

Ghourchian H.

autor

Ahmad F.

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