Effect of Cadmium Ion on alpha-Glucosidase: An Inhibition Kinetics and Molecular Dynamics Simulation Integration Study.
Protein J
; 35(3): 218-24, 2016 06.
Article
en En
| MEDLINE
| ID: mdl-27145787
ABSTRACT
α-Glucosidase is a critical metabolic enzyme that produces glucose molecules by catalyzing carbohydrates. The aim of this study is to elucidate biological toxicity of Cd(2+) based on α-glucosidase activity and conformational changes. We studied Cd(2+)-mediated inactivation as well as conformational modulation of α-glucosidase by using kinetics coupled with simulation of molecular dynamics. The enzyme was significantly inactivated by Cd(2+) in a reversibly binding behavior, and Cd(2+) binding induced a non-competitive type of inhibition reaction (the K i was calculated as 0.3863 ± 0.033 mM). Cd(2+) also modulated regional denaturation of the active site pocket as well as overall partial tertiary structural change. In computational simulations using molecular dynamics, simulated introduction of Cd(2+) induced in a depletion of secondary structure by docking Cd(2+) near the saccharides degradation at the active site, suggesting that Cd(2+) modulating enzyme denaturation. The present study elucidated that the binding of Cd(2+) triggers conformational changes of α-glucosidase as well as inactivates catalytic function, and thus suggests an explanation of the deleterious effects of Cd(2+) on α-glucosidase.
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Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
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Cadmio
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Contaminantes Ambientales
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Alfa-Glucosidasas
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Inhibidores de Glicósido Hidrolasas
Idioma:
En
Revista:
Protein J
Asunto de la revista:
BIOQUIMICA
Año:
2016
Tipo del documento:
Article