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Chemphyschem ; 24(24): e202300628, 2023 Dec 14.
Artigo em Inglês | MEDLINE | ID: mdl-37782219

RESUMO

The catalytic mechanism of a C a + 2 ${C{a}^{+2}}$ -dependent family 92 α ${{\rm \alpha }}$ -mannosidase, which is abundantly present in human gut flora and malfunctions leading to the lysosomal storage disease α-mannosidosis, has been investigated using quantum mechanics/molecular mechanics and metadynamics methods. Computational efforts show that the enzyme follows a conformational itinerary of and the C a + 2 ${C{a}^{+2}}$ ion serves a dual purpose, as it not only distorts the sugar ring but also plays a crucial role in orchestrating the arrangement of catalytic residues. This orchestration, in turn, contributes to the facilitation of O S 2 ${{{\rm \ }}^{{\rm O}}{{\rm S}}_{2}}$ conformers for the ensuing reaction. This mechanistic insight is well-aligned with the experimental predictions of the catalytic pathway, and the computed energies are of the same order of magnitude as the experimental estimations. Hence, our results extend the mechanistic understanding of glycosidases.


Assuntos
Manosidases , Simulação de Dinâmica Molecular , alfa-Manosidose , Catálise , Manosidases/química , Conformação Molecular , Microbioma Gastrointestinal/fisiologia , alfa-Manosidose/metabolismo , alfa-Manosidose/microbiologia , Proteínas de Bactérias/química , Proteínas de Bactérias/metabolismo
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