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Updated: Jan 31, 2026

Customization of Aspergillus niger Morphology Through Addition of Talc Micro Particles
Published on: March 15, 2012
Hidden Conformations in Aspergillus niger Monoamine Oxidase are Key for Catalytic Efficiency
Christian Curado-Carballada1, Ferran Feixas1, Javier Iglesias-Fernández1
1Institut de Química Computacional i Catàlisi (IQCC), Departament de Química, Carrer Maria Aurèlia Capmany 69, 17003, Girona, Catalonia, Spain.
Abstract:
Enzymes exist as an ensemble of conformational states, whose populations can be shifted by substrate binding, allosteric interactions, but also by introducing mutations to their sequence. Tuning the populations of the enzyme conformational states through mutation enables evolution towards novel activity. Herein, Markov state models are used to unveil hidden conformational states of monoamine oxidase from Aspergillus niger (MAO-N). These hidden conformations, not previously observed by any other technique, play a crucial role in substrate binding and enzyme activity. This reveals how distal mutations regulate MAO-N activity by stabilizing these hidden, catalytically important conformational states, but also by modulating the communication pathway between both MAO-N subunits.
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